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Ligand Co2+
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Basic Ligand Information
Related pathways
BRENDA
KEGG
MetaCyc
cob(II)yrinate a,c-diamide biosynthesis I (early cobalt insertion), cob(II)yrinate a,c-diamide biosynthesis II (late cobalt incorporation)
Show all BRENDA pathways known for Co2+
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (28 results)
top
EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + H+
ATP + hydrogenobyrinate a,c-diamide + Co2+ + H2O = ADP + phosphate + cob(II)yrinate a,c-diamide + H+
-
ATP + hydrogenobyrinic acid a,c-diamide + Co2+ + H2O = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
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ATP + hydrogenobyrinic acid a,c-diamide + Co2+ = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
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hydrogenobyrinic acid a,c-diamide + ATP + Co2+ = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
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In Vivo Product in Enzyme-catalyzed Reactions (5 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Substrate in Enzyme-catalyzed Reactions (54 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + sirohydrochlorin + Co2+ = ADP + phosphate + Co(II)-sirohydrochlorin + H+
ATP + sirohydrochlorin + Co2+ = ADP + phosphate + Co(II)-sirohydrochlorin + H+
ATP + sirohydrochlorin + Co2+ = ADP + phosphate + Co(II)-sirohydrochlorin + H+
ATP + sirohydrochlorin + Co2+ = ADP + phosphate + Co(II)-sirohydrochlorin + H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+
ATP + hydrogenobyrinate a,c-diamide + Co2+ + H2O = ADP + phosphate + cob(II)yrinate a,c-diamide + H+
-
ATP + hydrogenobyrinic acid a,c-diamide + Co2+ + H2O = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
-
ATP + hydrogenobyrinic acid a,c-diamide + Co2+ = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
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CTP + hydrogenobyrinic acid a,c-diamide + Co2+ = CDP + phosphate + cob(II)yrinic acid a,c-diamide + H+
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dATP + hydrogenobyrinic acid a,c-diamide + Co2+ = dADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
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hydrogenobyrinic acid a,c-diamide + ATP + Co2+ = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
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ITP + hydrogenobyrinic acid a,c-diamide + Co2+ = IDP + phosphate + cob(II)yrinic acid a,c-diamide + H+
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Product in Enzyme-catalyzed Reactions (9 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Activator in Enzyme-catalyzed Reactions (50 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
cobalt nanoparticles with particle size less than 50 nm significantly activate the enzyme in the serum, liver, and kidney of rats at concentration-dependent order with a maximum activation of 175% at 10 mM
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no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
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1.4fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM
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663.89% relative activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme, 536.91% relative activity of HQSA pretreated enzyme, consequently, the enzyme is incubated with Co2+ before activity assays
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about 60% activity in the presence of Mn2+ compared to 2-mercaptoethanol
Inhibitor in Enzyme-catalyzed Reactions (2699 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
at concentrations below 4 mM in presence of H2O2 competitive inhibitor to Mn2+, slightly stimulates NaN3 or alkylhydrazine inactivation
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10 mM, 17% loss of activity, isoenzyme FP2; 10 mM, 42% loss of activity, isoenzyme FP1; 10 mM, 53% loss of activity, isoenzyme FP3
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5 mM, 79% inhibition of cationic peroxidase GCP1. 5 mM, 20% inhibition of anionic peroxidase GCP2
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active site binding structure analysis, in both Co(II)-bound structures, in addition to the catalytic triad residues and 2-oxoglutarate or, malonate that coordinate cobalt, the remaining coordinate sites are occupied by water molecules thus forming a six-coordinate cobalt complex
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complete inhibition competitive to Fe2+, but stabilizes the enzyme against self-inactivation in absence of proclavaminate
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has an activating on multiple histone modifications at the global level. Cobalt ions significantly increase global histone H3K4me3, H3K9me2, H3K9me3, H3K27me3 and H3K36me3, as well as uH2A and uH2B and decreases acetylation at histone H4 (AcH4) in vivo. Cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process in vivo. And cobalt ions directly inhibit demethylase activity of JMJD2A in vitro. Cobalt ions do not increase the level of uH2A in the in vitro histone ubiquitinating assay and inhibit histone-deubiquitinating enzyme activity in vitro
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has an activating on multiple histone modifications at the global level. Cobalt ions significantly increase global histone H3K4me3, H3K9me2, H3K9me3, H3K27me3 and H3K36me3, as well as uH2A and uH2B and decreases acetylation at histone H4 (AcH4) in vivo. Cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process in vivo. And cobalt ions directly inhibit demethylase activity of JMJD2A in vitro. Cobalt ions do not increase the level of uH2A in the in vitro histone ubiquitinating assay and inhibit histone-deubiquitinating enzyme activity in vitro
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1 mM, isozyme A, 71% inhibition, isozyme B, 51% inhibition, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3
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inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
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there is a sharp decrease in activity when 1 mM Co2+ is added to the reaction assay
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inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
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inhibits TNMT activity by 71%, can be prevented by the inclusion of EDTA; inhibits activity by 71%, inhibition prevented by inclusion of 10 mM EDTA
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divalent cations at concentrations of more than 5 mM are inhibitory, 10 mM, total inhibition
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2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
inhibits the free enzyme by about 70% and the immobilized enzyme by about 15% at 5 mM
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the wild type enzyme shows complete inhibition at 3 mM. The C-terminally truncated enzyme shows about 28% residual activity at 10 mM
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1 mM, 98% inhibition with quercetin as substrate, 85% inhibition with gossypetin as substrate
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complete inhibition near 0.04 mM, UGT71F1; complete inhibition near 0.04 mM, UGT73A4
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the addition of 5 mM Co2+ reduces the activation by 5 mM MnCl2 of the enzyme by 45%; the addition of 5 mM Co2+ reduces the activation by 5 mM MnCl2 of the enzyme by 76%
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inhibition by binding to 2 types of metal ion sites, one type consists of a single site and has a low apparent affinity to Ca2+, at the remaining site(s), Ca2+ has a much higher apparent affinity than Zn2+, Ni2+ or Co2+ and prevents inhibition by these metal ions
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strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation
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order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
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complete inhibition in the forward reaction, strong inhibition in the reverse reaction
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no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
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isoyzme SCO1725 shows 93% residual activity in the presence of 10 mM Co2+; isozyme SCO7513 shows 72% residual activity in the presence of 10 mM Co2+
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significant inhibition of the intracellular enzyme, and slight inhibition of extracellular enzyme at 5 mM
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60% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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IC50: 0.029 mM, reaction with phosphatidic acid. IC50: 1.1 mM, reaction with diacylglycerol diphosphate. IC50: 1.2 mM, reaction with lysophosphatidic acid
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60% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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FS-44: 5'-PDase activity of bifunctional enzyme: cyclic-ribonucleotide phosphomutase-5'-phosphodiesterase
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1 mM, pH 8.0, 24 h at 4°C, 92% and 93% residual activity for Amy I and Amy II, respectively
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96% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
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1 mM, 22% inhibition of VpChiA, 15% inhibition of mutant enzyme VpChiAG589
isoforms Am0705 and Am2085 show complete inhibition at 2 mM Co2+, whereas isoforms Am0707 and Am1757 can maintain more than 60% of their enzymatic activities
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1 mM, pH 5.0, 95°C, 24% inhibition of hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
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50% reduction in alpha-mannosidase activity is observed after addition of 3 mM CoCl2
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50% inhibition at 50 mM for beta-D-fucosidase I, 22% inhibition for beta-D-fucosidase II
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5 mM, complete loss of activity, substrate: soluble starch; 5 mM, no residual activity
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about 70% residual activity at 10 mM, in the presence of 10% (w/v) NaCl
complete inhibition of xylanase II at 10 mM, 50% at 2 mM, no inhibition of xylanase I
in the presence of 10 mM, the relative xylanase activity decreases by 5%
30 min at 30ºC, 1 mM, 17% inhibition; 30 min at 30ºC, 10 mM, 70% inhibition; 30 min at 30ºC, 5 mM, 39% inhibition
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about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
at 1 mM, isoforms agarase-a and agarase-b show 81.31% and 91.81% residual activity, respectively
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24.2% residual activity at 0.1 M using inosine as substrate, 25.8% residual activity at 0.1 M using guanosine as substrate, 33.3% residual activity at 0.1 M using adenosine as substrate
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25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited, IC50: 0.1 mM
7-DMATS, FgaPT1, and CdpNPT show 10.2%, 32.3%, and 46.9% relative activity at 5 mM Co2+, respectively
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in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
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hydrolysis of the relative poor substrates, Pro-Gly and Gly-Gly is activated, whereas that of Ala-Gly is inhibited
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when substrates are cleaved rapidly by dipeptidase, addition of Co2+ inhibits the reaction. The more slowly a substrate is hydrolyzed in the absence of metals, the greater the activating effect
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at 37°C and pH of 7.5, 1 mM reduces prosubtilisin JB1 relative activity to 14% and 5 mM reduces prosubtilisin JB1 relative activity to 24%
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order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+, 50% inhibition at 0.25 mM
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
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5 mM, 46% loss of activity (soluble enzyme), 30% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
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competitive, 72% inhibition at 18 mM, partial protection or reverse effect by Ca2+ at 0.5 mM, Co2+ show partly Ca2+-sensitive and partly Ca2+-insensitive inhibition, molecular mechanism, Co21 accelerates the autolysis, overview
increases the activity 3-4fold at up to 2 mM, but inhibits at 2-18 mM, activation-and-inhibition dual effects of Co2+ ion are analysed kinetically
10 mM, 30% decrease of activity of enzyme produced with pET vector system and 20% decrease of activity of enzyme produced with pBAD vector system
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0.01 mM Co2+ inhibits the activity by 80%, while increasing concentrations rescue the lost activity
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promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
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40% residual activity at 1 mM for IsoI and 30% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII
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inhibition by elimination of the required metal-free GTP when present at high concentration with respect to the GTP concentration, overview
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can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
40% inhibition of the purified enzyme at concentration of 0.33 mM, activity in crude extract not affected
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supports D10p catalytic activity, but fails to demonstrate a synergistic effect on the enzyme when tested with Mn2+ ions
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rapid decreases in relative enzyme activity at 2 mM. The enzyme activity is completely lost at 16 mM
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10 mM, 67% inhibition of enzyme from cell line R-15, 33% inhibition of enzyme from cell line R-20
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substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components
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causes over 80% inhibition at 5 mM; causes over 80% inhibition at 5 mM; causes over 80% inhibition at 5 mM
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10 mM, complete inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+
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the addition of ethylene inhibitors decreases AtIRT1 expression, ethylene could be involved in the regulation of AtIRT1 transcription
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the addition of ethylene inhibitors decreases LeIRT1 expression, ethylene could be involved in the regulation of LeIRT1 transcription
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Metals and Ions (9539 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview
activates, a divalent cation is required for activity, can partially substitute for Mn2+
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at 0.002 mM MgCl2 enzyme activity is reduced to 25% without additional divalent cations, activity is restored with 0.5 or 5.0 mM CoCl2
-
addition of Co2+ restores activity of the zinc-dependent enzyme after inhibition by EDTA
-
moderately activating the reduction of butanal, but no activation of oxidation of 1-butanol
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Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
-
divalent cation required, at 0.5 mM Mn2+ causes optimal stimulation followed by Mg2+ and Co2+
-
divalent cations required 0.5 mM, Co2+ is 73% as effective as Mn2+ or Co2+
-
contains 0.35 mol of cobalt ions per mol of enzyme. Addition of 0.1 mM CoCl2 results in 2.1fold increase in activity
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
-
Co2+ salt addition increases the activity of quercetin 2,3-dioxygenase 24fold. The Escherichia coli cultures were grown at 37°C and 200 rpm for 6 h, induced with isopropyl beta-D-thiogalactopyanoside to a final concentraton of 50 mg/l in the presence of 10 microM CoCl2, and allow to grow additional 4 h at 25°C. The protein contains 0.65-0.8 atom of cobalt and 0.1 atom of iron per subunit.
supplementing the cultures of strain FLA with CoCl2 results in 1.6fold higher quercetinase activity in crude extracts
apoenzyme is catalytically inactive. Addition of Ni2+ or Co2+ yields activity. Production in intact Escherichia coli of E-2' depends on the availability of the Fe2+. Enzyme contains 1.1 Ni2+ per enzyme molecule
-
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
-
quantum-classical dynamics simulations with Co2+ bound. both Fe2+-like (reaction of EC 1.13.11.54) and Ni2+-like (reaction of EC 1.13.11.53) routes are accessible to Co2+-ARD, but the mechanism involves a bifurcating transition state, and so the exact product distribution is determined by the reaction dynamics
-
quantum-classical dynamics simulations with Co2+ bound. both Fe2+-like (reaction of EC 1.13.11.54) and Ni2+-like (reaction of EC 1.13.11.53) routes are accessible to Co2+-ARD, but the mechanism involves a bifurcating transition state, and so the exact product distribution is determined by the reaction dynamics
isothermal titration calorimetry and related biophysical techniques are used to generate complete thermodynamic profiles of Mn2+ and Co2+ binding to the 2-His-1-carboxylate facial triad of TauD
-
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+
-
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
particulate methane monooxygenase contains only mononuclear copper centers. Copper active sites structure analysis and measurement of Cu-Cu distances in the different sites, overview
-
required, a copper-dependent enzyme with three copper-binding sites. The ligands to two monocopper sites located in PmoB, the bis-His site and the CuB site, are not conserved, with the bis-His site only present in pMMOs of Gammaproteobacteria and the CuB site missing in pMMOs of Verrucomicrobia. By contrast, one aspartic acid and two histidine ligands to the third site, CuC, located in PmoC, are strictly conserved. The copper active site is located in PmoC. The bis-His site is coordinated by residues His48 and His72. Modeling of copper sites in the PmoB subunit of Methylococcus capsulatus pMMO, structure-function analysis, overview
-
enzyme requires adenosylcobalamin as a cofactor, the Co ion is involved in the reaction
-
Co2+ and Mn2+, at 0.5 mM, lower the content of isopentenyl diphosphate in the mixture of both products, isopentenyl diphosphate and dimethylallyl diphosphate
-
divalent cation requirement is satisfied by Co2+, is best supported by concentrations of divalent cation one-half the concentration of ATP
-
0.1 mM, 83% inhibition of the exchange of glycine carboxyl carbon with CO, catalyzed by glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein)
-
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
enzyme reconstituted with Co2+ exhibits 2.2% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable
0.15 mM, about 2fold increase of the rate of methylation of caffeoyl-CoA. Replacing Co2+ for Mg2+ drastically shifts the substrate preferences towards caffeic, 5-hydroxyferulic and 3,4-dihydroxybenzoic acid, which are not at all accepted in assays with Mg2+ as cofactor
-
Co2+ results in recovery of 82% of OMT-15 and 41% of OMT-17 activity compared to the addition of Mg2+
-
absolute requirement for the presence of a metal ion within the tetrapyrrole substrate
-
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 41% of the activity with Mg2+ (with quercetin as substrate)
-
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 82% of the activity with Mg2+ (with quercetin as substrate)
-
CdhE contains approximately 4.5 mol of Fe, 2.7 mol of acid-labile sulfur, and 0.3 mol of hydroxocobalamin per mol of purified CdhE
-
required, the apoprotein reacts with zinc or cobalt to the fully active holoenzyme
-
reconstitution of apo-enzyme with Co2+ yields an enzyme with 16fold higher specific activity, cysteine thiolate coordination in approximate tetrahedral geometry indicated by strong d-d transition absorbance centered at 622 nm, overview
-
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 41% of the activity with Mg2+ (with quercetin as substrate)
-
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 82% of the activity with Mg2+ (with quercetin as substrate)
-
substitution of magnesium for cobalt enhances the catalytic activity up to 40-100% for all RNA substrates
-
Co2+ results in recovery of 82% of OMT-15 and 41% of OMT-17 activity compared to the addition of Mg2+
-
metal-free enzyme preparation has no activity, addition of Co+ restores 46% of the original activity
-
Ni2+, and Co2+ also recover methylation activity by approximately 20-60% compared to that with Mg2+
-
Km: 0.33 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
-
substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
-
3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+
3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+
3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+
3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+
3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+
3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+
stimulates phospholipase reaction and cholesterol esterification, EDTA suppresses stimulation
-
enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be restored partially by Co2+ or Mn2+
enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be restored partially by Co2+ or Mn2+
enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be restored partially by Co2+ or Mn2+
enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be restored partially by Co2+ or Mn2+
enzymatic activity of LiCMS in the absence and presence of different metal ions. Co2+ is an activator
-
divalent cations are indispensable for the enzyme, acttivation by Co2+ is about 60% as compared to activation by Mn2+
-
the enzyme in testicular fluid has an absolute requirement for either Co2+, or Mn2+, Mg2+ and ca2+. The activity is stimulated by the cations in the above order. The enzyme from cauda epididymal fluid has an absolute requirement for Mn2+ or Ca2+, with Co2+ and Mg2+ being ineffective
-
divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
-
divalent cation required, maximum stimulation in presence of Ca2+. Co2+, Mg2+ or Mn2+ can replace Ca2+
-
stimulation at 10 mM is 25% of the stimulation with Mn2+. No further activation when the concentration is increased up to 50 mM
-
the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.91fold activation by 10 mM Co2+
-
divalent cation required, chitin synthase 2 shows highest activity with chitin synthase 2
-
in stimulation of Chs2 Co2+ is twice as effective on an enzyme activated by trypsin
-
18% and 39% of the wild-type GlcUA-transferase and GlcNAc-transferase activity with Mn2+, respectively, 0.2 mM
-
effect of divalent cations on MpgS activity decreases in the following order Mg2+, Co2+, Mn2+
17% and 31% as effective as Mn2+ for glucuronyltransferase and N-acetylgalactosaminyltransferase activities, respectively
-
strictly dependent on divalent cations in the following order of efficiency: Mn2+, Co2+, Mg2+. Maximal activity at 1 mM
-
strictly dependent on divalent cations, in the following order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
-
the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect
-
not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency
-
cobalt(II)-acetate supports glucosyltransferase activity but much less than with MnCl2
-
addition of cation stimulates, efficiency in descending order: Mn2+, Co2+, Mg2+, Fe2+, Ca2+, Ni2+, K+, Na+
-
requires divalent cation, in decreasing order of effectiveness: Mg2+, Ba2+, Ca2+, Co2+, relative activities: Mg2+: 1.0, Ba2+: 0.77, Ca2+: 0.65, Co2+: 0.31
-
activates at low but inhibits at high concentrations, optimal concentration: 0.3 mM, 80% as effective as 0.01 mM Mn2+
-
Mn2+ is the most effective metal cofactor, partial replacement with Co2+, Mg2+ and Ca2+, optimal concentration: 2.5 mM
-
10 mM, enzyme from gastric mucosa: 48.6% of the activation with Mn2+, enzyme from plasma: 94.3% of the activation with Mn2+
-
the enzyme is active in absence of divalent metal ions, but is stimulated by Mn2+, Mg2+, Ca2+ or Co2+
-
UPRTase can use Mn2+, Co2+ and Zn2+ instead of Mg2+. While the saturation curve for Mg2+ is smoothly increasing, these three metal ions are inhibitory at higher concentrations
-
with dimethylallyl diphosphate and isopentenyl diphosphate the enzyme is far more active with Co2+ as an additive than with any other tested metal ion. In the presence of Co2+ or Mn2+, with dimethylallyl diphosphate as a cosubstrate, the enzyme produces about 96% geranyl diphosphate and only 4% farnesyl diphosphate. In contrast, with Mg2+ as an additive, PcIDS1 produces 18% geranyl diphosphate and 82% farnesyl diphosphate
-
with dimethylallyl diphosphate and isopentenyl diphosphate the enzyme is far more active with Co2+ as an additive than with any other tested metal ion. In the presence of Co2+ or Mn2+, with dimethylallyl diphosphate as a cosubstrate, the enzyme produces about 96% geranyl diphosphate and only 4% farnesyl diphosphate. In contrast, with Mg2+ as an additive, PcIDS1 produces 18% geranyl diphosphate and 82% farnesyl diphosphate
-
enzyme depends absolutely on divalent cations in the descending order Mg2+, Mn2+, Co2+, 39% of the activity with Mg2+, KD: 0.27 mM
-
tetradentate coordination for the cobalt ion, binding structure, overview. In the four-coordinate state, the lower ligand and entire nucleotide arm are displaced by Phe91 and Trp93 and the N-terminal helix from the opposing subunit. This yields a closed active site or conformation for the enzyme. Relative to the five-coordinate cob(II)alamin state, this displacement involves a conformational change in the loop that extends from Met87 to Cys105 and includes a change in the orientation of Phe91 and Trp93
-
the enzyme requires Mg2+ and is inactive in the absence of metal. Optimal concentration of Mg2+ is 0.1 mM. Co2+ and Mn2+ activate the synthesis of farnesyl diphosphat at lower concentrations (0.005-0.05 mM) than does Mg2+ (0.05-0.5 mM). The enzyme also utilizes Ca2+, Ni2+, and Zn2+ as cofactors, but only at low concentrations (0.001-0.05 mM)
enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+
-
2fold lower inhibition by fosmidomycin with Co2+ as cofactor than with Mn2+ or Fe2+, no effect with sulfoenolpyruvate 7 as potential inhibitor
2fold lower inhibition by fosmidomycin with Co2+ as cofactor than with Mn2+ or Fe2+, no effect with sulfoenolpyruvate 7 as potential inhibitor
2fold lower inhibition by fosmidomycin with Co2+ as cofactor than with Mn2+ or Fe2+, no effect with sulfoenolpyruvate 7 as potential inhibitor
2fold lower inhibition by fosmidomycin with Co2+ as cofactor than with Mn2+ or Fe2+, no effect with sulfoenolpyruvate 7 as potential inhibitor
90.6% increase of activity at 2 mM for isozyme NCgl0950 DAHP synthase, 31.8% increase of activity at 2 mM for isozyme NCgl2098 DAHP synthase
90.6% increase of activity at 2 mM for isozyme NCgl0950 DAHP synthase, 31.8% increase of activity at 2 mM for isozyme NCgl2098 DAHP synthase
90.6% increase of activity at 2 mM for isozyme NCgl0950 DAHP synthase, 31.8% increase of activity at 2 mM for isozyme NCgl2098 DAHP synthase
90.6% increase of activity at 2 mM for isozyme NCgl0950 DAHP synthase, 31.8% increase of activity at 2 mM for isozyme NCgl2098 DAHP synthase
absolute requirement for divalent metal, 70% of the activation with Mg2+
absolute requirement for divalent metal, 70% of the activation with Mg2+
absolute requirement for divalent metal, 70% of the activation with Mg2+
absolute requirement for divalent metal, 70% of the activation with Mg2+
isoenzyme Ds-Co has an absolute requirement for divalent cations, Co2+ being best
isoenzyme Ds-Co has an absolute requirement for divalent cations, Co2+ being best
isoenzyme Ds-Co has an absolute requirement for divalent cations, Co2+ being best
isoenzyme Ds-Co has an absolute requirement for divalent cations, Co2+ being best
no activation of wild type enzyme, adverse effect on mutant N23C, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
-
1 mM stimulates around 2fold, the enzyme is dependent on the presence of metal ions such as Mg2+, Mn2+ or Co2+
-
evidence for a catalytically relevant interaction between the metal ion and the protein substrate in the enzyme
-
can replace Mg2+ with a lower relative activity, S-adenosylmethionine synthetase B
Co2+-dependent metalloenzyme. Co2+ contributes to the activity and selectivity of the enzyme. Highest activity when the Co2+ concentration is 6 to 10 mM. Specific activity of the enzyme with 6 mM Co2+ is 1.7fold than that of 1 mM Co2+
for maximal activation the cation concentration must be at least equal to ATP concentration
with MgCl2 nonaprenyl diphosphate is the longest product, with MnCl2 or CoCl2, the longest products are C50 and C55, respectively, partially purified enzyme
-
pseudaminic acid synthase requires the presence of a divalent metal ion for catalysis. The highest values are observed in the presence of Mn2+ and Co2+ (10 mM)
-
no activity is detected without a divalent cation. 100, 153, and 80% relative activity in the presence of Mg2+, Co2+, and Mn2+, respectively, at 4 mM
-
metal-ion dependent enzyme, highest activity (5.09 mM/min*mg) in presence of Co2+ followed by Mg2+ (3.28 mM/min*mg) at 90°C and pH 7.5
no enzyme activity in the absence of divalent cations. Co2+ can replace Mg2+ with 35% of the maximal activity obtained in presence of Mg2+
2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 70% compared to the activation with Mg2+, activation of glucokinase activity is about 35% compared to the activation with Mg2+
-
metal-ion dependent enzyme, highest activity (5.09 mM/min*mg) in presence of Co2+ followed by Mg2+ (3.28 mM/min*mg) at 90°C and pH 7.5
-
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
-
2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 70% compared to the activation with Mg2+, activation of glucokinase activity is about 35% compared to the activation with Mg2+
-
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
-
can replace Mg2+ in activation, optimal concentration: 5 mM, 87% of the activity with Mg2+
-
the enzyme is dependent on monovalent as well as divalent cations for its catalytic activity. When magnesium is substituted with Co2+ and Mn2+ in the reaction mixture, the ribokinase activity got reduced to 60% and 45% as compared to that with Mg2+
-
divalent cation required, efficiency in descending order: Mg2+ > Mn2+ > Co2+, optimum Co2+ concentration is 10 mM, maximal activity is 50% of that with Mg2+
-
divalent metal ion required, maximal activity in presence of Co2+ or Mg2+ (10 mM)
-
activity is dependent on divalent cation. Activity is highest in presence of Mg2+ (5 mM) or Fe2+ (5 mM). 70% of maximal activation with Mn2+ (5 mM) or Ca2+ (5 mM). 35% of maximal activation with Co2+ (5 mM) or Zn2+ (5 mM)
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
-
0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively, inhibitory in excess
-
divalent metal ions are essential activators, in the order of decreasing efficiency: Mg2+, Co2+, Zn2+, Cu2+, Cd2+, Fe2+
-
divalent cation requirement satisfied by 0.1 M Mg2+ or Co2+ and partially satisfied by Mn2+, Fe2+ or Ca2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
-
divalent cation required, efficiency of activation in descending order: Mg2+, Mn2+, Zn2+, Co2+
-
divalent cation required, at 1 mM Co2+ activation results in 120% of the activity with Mg2+
-
divalent cation required, at 1 mM Co2+ activation results in 170% of the activity with Mg2+
-
divalent cation required, at 1 mM Co2+ activation results in 80% of the activity with Mn2+
-
multiphasical activation, at pH below physiological value, inhibits at physiological pH
-
divalent cation required, Co2+ stimulates with maximal activity at 3-5 mM, maximal activity is about 35-30% compared to activation by Mg2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Co2+, Mn2+, Fe2+
-
divalent cations activate in the order of decreasing efficiency: Mn2+, Mg2+, Ca2+, Fe2+
-
divalent cation required, 86% of the activity with Mg2+ for the polyphosphate-dependent activity and 30% of the activity with Mg2+ for ATP-dependent activity, 5 mM
-
divalent cations activate in the order of decreasing effectiveness: Mg2+, Mn2+, Co2+, Zn2+
-
can partially replace Mg2+ in activation, 25% of the activation with Mg2+, optimal concentration is 10 mM
-
divalent metal ions stimulate in decreasing order of efficiency: Mg2+, Fe2+, Mn2+, Fe3+, Co2+
-
activates, 86% and 30% activity with polyphosphate and ATP, respectively, compared to Mg2+
-
divalent cation required, Mg2+ and Mn2+ are most effective, Co2+ activates to a lesser extent
-
divalent cations required, Mg2+ is most effective, but significant activity is obtained with Fe2+, Ca2+, Mn2+ or Co2+, isoenzyme SK2
-
2 mM, activity with AMP and deoxythymidine is enhanced about 50%, no absolute requirement
-
enhances phosphatase activity considerably, but transferase activity to a small extent
-
at low concentration (0.01 mM), Co2+ ions can replace Mg2+ (about 39% of the Mg2+ activity)
-
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)
-
enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+
-
requirement, 1-10 mM, can replace Mg2+ to some extent, inhibits above 30 mM
requirement, 1-10 mM, can replace Mg2+ to some extent, inhibits above 30 mM
requirement, 1-10 mM, can replace Mg2+ to some extent, inhibits above 30 mM
requirement, 1-10 mM, can replace Mg2+ to some extent, inhibits above 30 mM
requirement, 1-10 mM, can replace Mg2+ to some extent, inhibits above 30 mM
requirement, 1-10 mM, can replace Mg2+ to some extent, inhibits above 30 mM
requirement, 1-10 mM, can replace Mg2+ to some extent, inhibits above 30 mM
requirement, 1-10 mM, can replace Mg2+ to some extent, inhibits above 30 mM
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
-
bivalent cation required, Mg2+ is the most commonly used, enzyme from Streptococcus lactis is also fully active with Mn2+ and less so with Fe2+ and Co2+
-
partially active in the presence of 5 mM Co2+, 23% compared to activity with 5 mM Mg2+
-
absolute requirement for a divalent cation such as Mg2+, Mn2+ or Co2+. In presence of 2 mM ATP maximal activity occurs with 1 mM Co2+
-
absolute requirement for a divalent metal ion, at pH 10.0 Mg2+ and Mn2+ are most effective, at pH 7.0 Mg2+, Co2+, Mn2+, Fe2+ and Zn2+ are effective
-
absolute requirement for bivalent cations, at pH 10.0 Mg2+ is most effective, while Mn2+, Co2+ and Zn2+ show little activity. At pH 7.0, Co2+ is most effective and Mg2+, Mn2+, Ni2+ and Fe2+ show little activity. Optimal concentration is 2.5 mM Co2+
-
10 mM, the enzyme requires divalent cations for the activity. MgCl2 is the most effective additive. can replace Mg2+ with 51% of the activity compared to 10 mM Mg2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2
-
metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
-
divalent cation required for activity, second best activator, maximal activation at 5 mM
-
the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+
-
Co2+ results in significant activity at a concentration of 25 mM, with 41% of the activity seen with 25 mM Mg2+, the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+
-
Co2+ induces FAD hydrolysis, which is strongly stimulated in the presence of K+, K0.5 value is 0.035 mM
-
in the presence of about 0.5 mM Co2+, the activity is almost equal to that measured with Mg2+
-
the enzyme requires divalent metals for activity, the best activity being observed with Co2+, where the activity is 4times greater than that with Mg2+
-
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation
-
absolute requirement for a divalent metal ion. Order of effectiveness is: Mn2+, Mg2+, Zn2+, Cu2+, Fe2+, Ni2+, Co2+
-
absolute requirement for divalent cation. Order of decreasing effectiveness is: Co2+, Mn2+, Mg2+, Zn2+
-
decreasing order of efficiency for elongation of oligonucleotide primers with dATP: Mg2+, Zn2+, Co2+
decreasing order of efficiency for elongation of oligonucleotide primers with dATP: Mg2+, Zn2+, Co2+
decreasing order of efficiency for elongation of oligonucleotide primers with dATP: Mg2+, Zn2+, Co2+
effect of Mn2+, Co2+ and Zn2+, analysis in X-ray structures that mimic the pre-catalytic state, the post-catalytic state and a competent state
effect of Mn2+, Co2+ and Zn2+, analysis in X-ray structures that mimic the pre-catalytic state, the post-catalytic state and a competent state
effect of Mn2+, Co2+ and Zn2+, analysis in X-ray structures that mimic the pre-catalytic state, the post-catalytic state and a competent state
human enzyme catalyzes the polymerization reaction as well or better in the presence of Mn2+ or Co2+ than in presence of Mg2+
human enzyme catalyzes the polymerization reaction as well or better in the presence of Mn2+ or Co2+ than in presence of Mg2+
human enzyme catalyzes the polymerization reaction as well or better in the presence of Mn2+ or Co2+ than in presence of Mg2+
with decreasing order of efficiency in CDPglucose synthesis: Co2+, Mn2+, Mg2+ can replace Mg2+ in diphosphorolysis
-
divalent metal ion is strictly required, with 20 mM Mn2+ 27% of the activation compared to activation by Mg2+
-
the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+
-
enzyme exhibits a strong preference to incorporate Sp-TTP alphaS isomer over Rp-TTP alphaS isomer in the presence of Mg2+. This stereoselective preference is decreased when Mg2+ is replaced with Mn2+ and Co2+
-
Rv2613c requires bivalent metal ions such as Co2+ to exert its Ap4A phosphorylase activity (68% activity in the presence of 2 mM Co2+)
-
can effectively replace Mg2+. When Mg2+ is replaced with Co2+, the efficiency of incorporation of dTMP opposite dA increases by 5-fold
can effectively replace Mg2+. When Mg2+ is replaced with Co2+, the efficiency of incorporation of dTMP opposite dA increases by 5-fold
can effectively replace Mg2+. When Mg2+ is replaced with Co2+, the efficiency of incorporation of dTMP opposite dA increases by 5-fold
can effectively replace Mg2+. When Mg2+ is replaced with Co2+, the efficiency of incorporation of dTMP opposite dA increases by 5-fold
can partially replace Mg2+ in activation, optimal concentration: 2.5 mM
can partially replace Mg2+ in activation, optimal concentration: 2.5 mM
can partially replace Mg2+ in activation, optimal concentration: 2.5 mM
can partially replace Mg2+ in activation, optimal concentration: 2.5 mM
the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Co2+ is 13% compared to the activity in presence of 10 mM Mg2+
-
activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
-
activates slightly, can only partly substitute for Mn2+. Co2+ is coordinated by the phosphate moiety and the carboxylate group of Glu224 as well as the carboxylate group of Asp171 and the imidazole ring nitrogen of His170 of the symmetry-related subunit
no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
-
most efficient cation for the activation. Co2+ activates cardiolipin formation by increasing the maximal enzyme activity from 2.9 pmol/min/mg protein at low Co2+ concentration to 4.1 pmol/min/mg protein at high Co2+ concentration
-
the enzyme displays an absolute requirement for divalent cations with Co2+ being more efficient than Mg2+ or Mn2+
-
the enzyme is dependent on the presence of bivalent cations. The largest activity is found with Co2+, whereas Mn2+ supports a lower activity. No detectable cardiolipin synthase activity when using Ni2+, Ca2+, or Mg2+
-
cation requirement is relatively nonspecific, Mg2+, Ba2+ or Ca2+ provides maximal activation in the 10 mM range, Mn2+ or Co2+ stimulates at lower concentration, inhibition at higher concentration
-
good activator, stimulates chondroitin 6-sulfotransferase activity and keratan sulfate sulfotransferase activity
-
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
-
the catalytic activity strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
-
112.56% increase in activity in the presence of 0.1 mM Co2+, the stimulatory effect is not observed at higher concentrations
-
activation, the vicinal hydroxyl group is prerequisite for metal activation of Clostridium thermocellum acetylxylan esterase
is required for catalysis. Enzyme activity increases by 54% on addition of 0.1 mM
metal ion-dependent enzyme, possesses a single metal center with a chemical preference for Co2+
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
contains a cobalt ion in the active site. 0.2 mM used in assay conditions
contains a cobalt ion in the active site. 0.2 mM used in assay conditions
contains a cobalt ion in the active site. 0.2 mM used in assay conditions
contains a cobalt ion in the active site. 0.2 mM used in assay conditions
contains a cobalt ion in the active site. 0.2 mM used in assay conditions
contains a cobalt ion in the active site. 0.2 mM used in assay conditions
required, VmoLac is a bi-cobalt metalloenzyme. The two metal cations are coordinated by four histidines, His23, His25, His171, and His200, an aspartic acid Asp257, and a carboxylated lysine residue Lys238
required, VmoLac is a bi-cobalt metalloenzyme. The two metal cations are coordinated by four histidines, His23, His25, His171, and His200, an aspartic acid Asp257, and a carboxylated lysine residue Lys238
required, VmoLac is a bi-cobalt metalloenzyme. The two metal cations are coordinated by four histidines, His23, His25, His171, and His200, an aspartic acid Asp257, and a carboxylated lysine residue Lys238
required, VmoLac is a bi-cobalt metalloenzyme. The two metal cations are coordinated by four histidines, His23, His25, His171, and His200, an aspartic acid Asp257, and a carboxylated lysine residue Lys238
required, VmoLac is a bi-cobalt metalloenzyme. The two metal cations are coordinated by four histidines, His23, His25, His171, and His200, an aspartic acid Asp257, and a carboxylated lysine residue Lys238
required, VmoLac is a bi-cobalt metalloenzyme. The two metal cations are coordinated by four histidines, His23, His25, His171, and His200, an aspartic acid Asp257, and a carboxylated lysine residue Lys238
significantly enhances the activity of AisZ and restores the EDTA-inactivated AisZ
significantly enhances the activity of AisZ and restores the EDTA-inactivated AisZ
significantly enhances the activity of AisZ and restores the EDTA-inactivated AisZ
significantly enhances the activity of AisZ and restores the EDTA-inactivated AisZ
significantly enhances the activity of AisZ and restores the EDTA-inactivated AisZ
significantly enhances the activity of AisZ and restores the EDTA-inactivated AisZ
1 mM, 106.3% relative activity as compared to activity in the absence of metal ion
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enzyme requires a divalent cation for activity. This requirement can be satisfied by Mg2+, Mn2+ or Co2+
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reaction performs mainly double strand scissions, Co2+ is a better activator than other divalent metals
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the enzyme exhibits a non-linear dependence in the presence of Co2+. The AP site cleavage activity increases from 0.1 to 0.5 mM and then rapidly decreases from 0.5 to 10 mM CoCl2
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can replace Mn2+ but yields a much lower activity than Mg2+, highest activity at 0.1 mM, inhibitory at high concentrations
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CoCl2 can substitute for MgCl2. The activity at the optimal Co2+ concentration (0.001 M) is 27% higher than that found at the optimal Mg2+ concentration
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Co2+ supplementation enhances the 3'-end processing efficiency by almost 3000fold
-
10 mM Co2+ supports activity, with only minor inhibition observed at higher concentrations
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divalent metal ion required. Maximal activity is obtained with 10 mM Mg2+, 5 mM Co2+ or 0.5 mM Mn2+
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divalent metal required, optimal concentration: 20 mM, 70% of the activity with Mg2+
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strictly metal-dependent nuclease. It exhibits activity in the presence of Mg2+, Mn2+, Co2+ or Ni2+, whereas no activity is observed in the absence of these metal ions. Optimum concentration of Co2+ or Ni2+ needed for aRNase HII activity is 1 mM. Little activity is detected in the presence of other metals including Co3+, Cu2+, Zn2+, and Ca2+
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the enzyme cleaves an RNA strand of the 12-bp RNA/DNA hybrid at multiple sites only in the presence of Mn2+, Mg2+, Co2+ or Ni2+, but not in the presence of Cu2+, Ca2+ or Zn2+, or in the absence of divalent metal ions. The enzyme cleaves an RNA/RNA duplex in the presence of Mn2+ or Co2+
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the enzyme exhibits the highest activity in the presence of 5 mM Mn2+, 1 mM Co2+, or 10 mM Mg2+, respectively. The specific activity of the enzyme determined with 5 mM MnCl2 is slightly higher than that determined with 10 mM MgCl2, and about 2 folds higher than that determined with 1 mM CoCl2
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26% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0022 mM for wild-type enzyme, 0.00051 mM for mutant os-1 enzyme
26% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0022 mM for wild-type enzyme, 0.00051 mM for mutant os-1 enzyme
50fold increase in activity compared with activity before EDTA treatment
50fold increase in activity compared with activity before EDTA treatment
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
activity is dependent on metal ion, Co2+ is the most active stimulator and has unique effect at high temperature
activity is dependent on metal ion, Co2+ is the most active stimulator and has unique effect at high temperature
metalloenzyme, dependent on, can partially be substituted by Mg2+ and Mn2+
metalloenzyme, dependent on, can partially be substituted by Mg2+ and Mn2+
required. In the absence of Co2+ in the lysis buffer, activity of extracts is only 10% of the normal value
required. In the absence of Co2+ in the lysis buffer, activity of extracts is only 10% of the normal value
similar levels of activity are detected in the presence of 1 mM Mg2+, Mn2+, and Ni2+
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enzyme is inactive in absence of a bivalent metal. Requirement is met most effectively by Mg2+ with Co2+, Fe2+ and Mn2+ serving much less adequately
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activity is dependent on the presence of divalent ions such as Mn2+, Co2+, Ni2+, or Mg2+. Mn2+, Co2+, Ni2+ are much more effective than Mg2+. Maximal activation is induced at concentrations in the range of 0.5 to 1 mM
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the enzyme requires a divalent metal ion for activity. The highest activity is observed with Cu2+, followed by Mn2+, Ni2+, Mg2+, Cd2+and Co2+, in the presence of EGTA. When EGTA is replaced by EDTA, activity can be observed. In the absence of divalent metal ions the enzyme is inactive
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35% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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activates, competitive binding to other metal ions, KM 0.0145 mM and turnover number 7.28 s-1 at pH 7.0, 30°C, recombinant enzyme
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activation is due to zinc ion displacement at only one of two metal-ion-binding sites, displacement occurs at the metal-ion bionding site consisting of the residues Asp84, Asn116, His217 and His252. Km for wild-type enzyme: 0.0925 mM
activation is due to zinc ion displacement at only one of two metal-ion-binding sites, displacement occurs at the metal-ion bionding site consisting of the residues Asp84, Asn116, His217 and His252. Km for wild-type enzyme: 0.0925 mM
KD: 46.9 +/- 5.66 microM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
KD: 46.9 +/- 5.66 microM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
activates, competitive binding to other metal ions, KM 0.0145 mM and turnover number 7.28 s-1 at pH 7.0, 30°C, recombinant enzyme
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5 mM, divalent cation required for maximal activity, doubles the rate of glucose 6-phosphate hydrolysis
-
KD: 46.9 +/- 5.66 microM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
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activity is strictly dependent on divalent cations. Mn2+, Co2+, Mg2+, and to a lesser extent Ni2+ activate the enzyme
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stimulates to a lesser extend than Mg2+, higher activity with phosphocholine than with phosphoethanolamine in the presence of Co2+ and Mn2+ most probably due to an allosteric effect caused by a difference in the metal-binding properties of each enzyme-substrate complex
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35% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
phytase hydrolyzes and liberates inorganic phosphate from Ca2+, Mg2+, and Co2+ phytates more efficiently than those of Al3+, Fe2+, Fe3+, and Zn2+
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at 50°C, divalent cations are absolutely required for GpgP activity with 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate as the substrate. However, when 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate is the substrate, 3% activity is detected without cations, and the preferred metal ion with both substrates is Co2+ (10 mM). At 30°C, GpgP retains 37% of its enzyme activity towards 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate and 12% activity towards 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate in a reaction mixture without cations compared to the activity with 10 mM K+ and Co2+
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stimulates activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate or 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
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presence of divalent cation absolutely required. Maximum activity with Co2+, followed in decreasing order by Mn2+, Cu2+. Apparent Kd value for Co2+ 0.8 mM
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strictly dependent on divalent cations in decreasing order of efficiency: Mg2+, Ni2+, Co2+
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10 mM, promotes junction cleavage, active site of endonuclease I has binding sites for two metal ions
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Km: 0.142 mM, activation of sphingomyelinase activity in the order of decreasing efficiency Co2+, Mn2+, Mg2+, Ca2+, Sr2+. There are three distinct metal ion-binding sites in a long horizontal cleft across the bc-SMase molecule
rank-order of increasing activation: Mg2+, Co2+, Mn2+, Zn2+. The four metal ions compete with each other for the same binding site on the enzyme molecule
PdeB is stimulated about 2fold by 0.05 mM Co2+, at pH 8.0 in 50 mM Tris-HCl buffer with cyclic 3',5'-AMP as substrate
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the enzyme activities of PdeA and PdeB in the hydrolysis of 3',5'-cAMP are stimulated 3.2fold and 1.98fold at pH 8.0 in 50 mM Tris-HCl buffer by the addition of Co2+ at 0.05 mM, respectively
the enzyme shows maximum activity at very low concentrations (less than 0.05 mM) of Co2+
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check the sensitivity to metals for the human and murine isoforms, concentrations ranging from 0.1 to 1000 mM
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lysoPLD activity is increased when Co2+ is added. Addition of Zn2+, Mn2+, Ni2+, or Co2+ to diluted egg white alters preference patterns of lysoPLD toward choline-containing substrates
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purified enzyme is incubated with Co2+. LysoPLD activity in serum is more sensitive to Co2+
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stimulation of enzyme activity and synthesis of COX-2 protein in time- and dose-dependent manner. Elevated expression of isoforms PLD1 and PLD2 increases hypoxia-induced COX-2 expression and prostaglandin E2 production. PLD1 enhances COX-2 expression by Co2+ via reactive oxygen species, p38 MAK kinase, PKC-delta, and PKA, but not ERK, whereas PLD2 enhances Co2+-induced COX-2 expression via reactive oxygen species and p38 MAP kinase, but not PKC-delta, PKA and ERK
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quantification of binding affinity. Metal ions bind to the six-coordinate alpha site of the protein in an entropically driven process with loss of a proton, while binding at the beta site is not detected. Phosphate enhances the metal affinity of the alpha site by increasing the binding entropy and the metal affinity of the beta site by enthalpic (Co) or entropic (Mn) contributions, but no additional loss of protons
quantification of binding affinity. Metal ions bind to the six-coordinate alpha site of the protein in an entropically driven process with loss of a proton, while binding at the beta site is not detected. Phosphate enhances the metal affinity of the alpha site by increasing the binding entropy and the metal affinity of the beta site by enthalpic (Co) or entropic (Mn) contributions, but no additional loss of protons
activity of is highest in the presence of Co2+ which is a bout 1.5 times higher than that of Mn2+ or twice than that of Mg2+, respectively. Ca2+, Fe2+, Ni2+, Zn2+ do not support activity
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the 3',5'-phosphodiesterase enzyme activities of PdeA and PdeB are stimulated 3.2fold and 1.98old, respectively, by 0.05 mM Co2+ at pH 8.0 in 50 mM Tris-HCl buffer
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stimulated up to 30fold by millimolar order of Ca2+. This effect is fully substituted by other divalent cations such as Co2+, Mg2+, Mn2+, Ba2+, Sr2+ and Ni2+
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0.75 mM Mn2+ shows a 6fold activation of hydrolysis of bis(4-nitrophenyl) phosphate
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Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor
-
Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor
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2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
in the crystal structure, the metal ion is present in a conserved octahedral coordination with conserved side chain atoms, the ligand atoms and an invariant water molecule
in the crystal structure, the metal ion is present in a conserved octahedral coordination with conserved side chain atoms, the ligand atoms and an invariant water molecule
in the crystal structure, the metal ion is present in a conserved octahedral coordination with conserved side chain atoms, the ligand atoms and an invariant water molecule
in the crystal structure, the metal ion is present in a conserved octahedral coordination with conserved side chain atoms, the ligand atoms and an invariant water molecule
in the crystal structure, the metal ion is present in a conserved octahedral coordination with conserved side chain atoms, the ligand atoms and an invariant water molecule
activates about 1.5fold at 5 mM, does not stabilize the purified recombinant enzyme
-
1 mM, 8.1fold stimulation of activity with o-nitrophenyl beta-D-galactopyranoside, 4.7fold stimulation of activity with lactose
-
8.3fold activation at a concentration of 10 mM, resistance of ManA to heat inactivation is increased by presence of Co2+
-
activates, purified enzyme carries two Co2+ ions, the enzyme treated with Co2+ carries four. Co2+ regulates the substrate specificity of the enzyme. The Co2+-treated enzyme produces Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]-Man-beta-(1-4)-GlcNAc and alpha-D-mannose as end products from Man-alpha-(1-2)-Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-3)]-Manalpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]-Man-beta(1-4)GlcNAc in presence of Co2+. Before tretament with Co2+ the enzyme is able to cleave a single Man-alpha-(1-2) residue from Man-alpha-(1-2)-Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-3)]-Manalpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]-Man-beta(1-4)GlcNAc to give Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha(1-3)]-Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha(1-3)]-Man-beta-(1-4)-GlcNAc as the end product
-
activation after preincubation at 1.4 mM, activation persists even after removal of Co2+
-
Co2+ is by far the most efficient metal ion in stimulating hydrolysis of 4-nitrophenyl alpha-D-mannoside. The side chains at positions 228 and 533 are involved in binding the activating metal ion as their primary function
-
enhances acivity, alpha-mannosidase in absence of Co2+ only converts mannosyl(9)-N-acetyl-glucosamine into mannosyl(8)-N-acetyl-glucosamine, in presence of Co2+, alpha-mannosidase yields mannosyl(5)-N-acetyl-glucosamine
-
maximal activity of 51 U/mg is reached at 1 mM CoCl2. Inactive in absence of metal ion
-
with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
-
5 mM, 3.3fold activation of activity with carboxymethyl cellulose, 1.4fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
5 mM, 3.3fold activation of activity with carboxymethyl cellulose, 1.4fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
activation by divalent cation up to 40% at 1 mM, in decreasing order of activation effect: Mg2+, Ni2+, Co2+, Ca2+, Mn2+ and Zn2+
requires Co2+ for activity. Cobalt is bound to the nucleosidase with a stoichiometry of 1 equivalent of cobalt/subunit
-
apoenzyme can be restored by addition of Co2+, peptidase activity exceeds that of enzyme reactivated with zinc
-
apoenzyme is inactive and can be reactivated by addition of stoichiometric amounts of zinc and cobalt
-
addition of the ion prior to mixing with substrate increases activity up to 24fold
-
metal-dependent enzyme. The active site metal ion is essential for catalytic activity. It has a secondary structural role mediating the formation of active hexamers. Mn2+ and Co2+ induce oligomerization. The enzyme exists in a metal-dependent dynamic equilibrium between active hexameric species and smaller inactive species that can be controlled by manipulating the identity and concentration of metals available. Mutation of residues involved in metal ion binding impaire catalytic activity and the formation of active hexamers. Structural resolution of Pv-M17 by cryoelectron microscopy and X-ray crystallography together with solution studies reveal that the enzyme binds metal ions and substrates in a conserved fashion
-
two Co2+ is bound per subunit in wild-type enzyme. One Co2+ is bound per subunit in mutant enzymes D62A, D62N and D62E
-
two ions per subunit, one exchangeable metal site can be occupied by Zn2+ or Mg2+, Co2+, or Mn2+, while the second, tight binding site can be occupied only by Zn2+ or Co2+, overview
-
2 Co2+ bound at the dinuclear active site, can be substituted by Zn2+, binding mode
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Co2+ can substitute for Zn2+ at the the dinuclear active site of the enzyme
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than the other way round, which suggests two metal-binding sites with different functions
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
spectroscopically distinct cobalt sites in heterodimetallic enzymes, implications for substrate binding
required, 0.93-1.25 mol cobalt per mol enzyme, optimal concentration 0.003-0.018 mM, involved in enzyme-substrate binding, inhibitory above 3-7 mM, time-course of activation
-
0.2 mM, 4fold stimulation. When the sample is preincubated with 0.2 mM Co2+ ions and subjected to gel filtration, only 10% of the activity remains, while addition of Co2+ (0.2 mM) to the reaction mixture completely restores enzyme activity. Co2+ions could not be replaced with other divalent (Ca2+, Cd2+, Cu2+, Fe2+, Mg2+, Mn2+, Ni2+, or Zn2+) or monovalent cations (Na+or K+) when used at concentrations of up to 0.2 mM
25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited
for spectroscopic studies the enzyme containing magnetically and spectroscopically silent Zn(II) ion is substituted with Co(II)
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme