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2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
2 ATP + 2 [corrinoid adenosyltransferase]-cob(I)alamin = 2 triphosphate + 2 adenosylcob(III)alamin + 2 [corrinoid adenosyltransferase]
(1c)
-
-
-
2 ATP + 2 [corrinoid adenosyltransferase]-cob(I)yrinic acid a,c-diamide = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + 2 [corrinoid adenosyltransferase]
(2c)
-
-
-
2 cob(II)alamin + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)alamin
(1a)
-
-
-
2 cob(II)yrinic acid a,c-diamide + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)yrinic acid a,c-diamide
(2a)
-
-
-
a reduced flavoprotein + 2 [corrinoid adenosyltransferase]-cob(II)alamin = an oxidized flavoprotein + 2 [corrinoid adenosyltransferase]-cob(I)alamin
(1b), spontaneous
-
-
-
a reduced flavoprotein + 2 [corrinoid adenosyltransferase]-cob(II)yrinic acid a,c-diamide = an oxidized flavoprotein + 2 [corrinoid adenosyltransferase]-cob(I)yrinic acid a,c-diamide
(2b), spontaneous
-
-
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
reaction mechanism
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
reaction mechanism, substrate structure
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
active site and substrate binding sites and structures, molecular architecture
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
Cys79, Cys80, and Cys83 are important for catalysis
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
nucleophilic attack from reduced Co1+ ion of cob(I)alamin to the C-5 carbon of ATP, ordered substrate binding mechanism with ATP being first and essential for catalysis
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
(1) overall reaction
-
-
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
residues Phe91 and Trp93 play a critical role in the mechanism of four-coordinate Cob(II)alamin formation in the active site of the Salmonella enterica ATP:Co(I)rrinoid adenosyltransferase enzyme, overview. The enzyme adopts a closed conformation and residues Phe91 and Trp93 displace 5,6-dimethylbenzimidazole, the lower nucleotide ligand base of cobalamin, to generate a transient four-coordinate cobalamin, which is critical in the formation of the AdoCbl Co-C bond, important role of bulky hydrophobic side chains in the active site. CobA and PduO increase the redox potential of the cob(II)alamin/cob(I)alamin couple to facilitate formation of the Co-C bond, in both cases the polar coordination of the lower ligand to the cobalt ion is eliminated by placing that face of the corrin ring adjacent to a cluster of bulky hydrophobic side chains
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
to overcome the thermodynamically challenging Co2+ -> Co1+ reduction, the enzyme drastically weakens the axial ligand-Co2+ bond so as to generate effectively four-coordinate Co2+-corrinoid species, mechanism, overview. The entire hydrophobic pocket below the corrin ring, and not just residue F112, is critical for the removal of the axial ligand from the cobalt center of the Co2+-corrinoids. Large role of the ATP-induced active-site conformational changes with respect to the formation of 4c Co(II)Cbl
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
active site and substrate binding sites and structures, molecular architecture
-
-
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
reaction mechanism
-
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
active site and substrate binding sites and structures, molecular architecture
-
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
Cys79, Cys80, and Cys83 are important for catalysis
-
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
not yet confimed
-
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
not yet confimed
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
residues Phe91 and Trp93 play a critical role in the mechanism of four-coordinate Cob(II)alamin formation in the active site of the Salmonella enterica ATP:Co(I)rrinoid adenosyltransferase enzyme, overview.. The enzyme adopts a closed conformation and residues Phe91 and Trp93 displace 5,6-dimethylbenzimidazole, the lower nucleotide ligand base of cobalamin, to generate a transient four-coordinate cobalamin, which is critical in the formation of the AdoCbl Co-C bond, important role of bulky hydrophobic side chains in the active site. CobA and PduO increase the redox potential of the cob(II)alamin/cob(I)alamin couple to facilitate formation of the Co-C bond, in both cases the polar coordination of the lower ligand to the cobalt ion is eliminated by placing that face of the corrin ring adjacent to a cluster of bulky hydrophobic side chains
-
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
(2) overall reaction
-
-
-
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
active site and substrate binding sites and structures, molecular architecture
-
-
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2 ATP + 2 cob(II)alamin + a reduced flavoprotein
2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
2'-deoxy-ATP + cob(I)alamin + H2O
?
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(I)alamine
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
ATP + cob(I)alamin
triphosphate + adenosylcobalamin
ATP + cob(I)alamin
triphosphate + coenzyme B12
ATP + cob(I)alamin
tripolyphosphate + coenzyme B12
ATP + cob(I)alamin + H2O
?
anaerobic, 20 min, 80°C, pH 8, in presence of 1 mM titanium (III) citrate
ATP-dependent cob(I)alamin consumption to a yet unknown compound
-
?
ATP + cob(I)alamin + H2O
adenosylcobalamin + diphosphate + phosphate
-
37°C
monitoring adenosylcobalamin formation at 388 nm in continous spectrophotometric assay
-
?
ATP + cob(I)alamin + H2O
phosphate + diphosphate + adenosylcobalamin
anaerobic, 20 min, 80°C, pH 8, in presence of 1 mM titanium (III) citrate
measured by decrease in light absorbance by cob(I)alamin at 388 nm and increase of light absorbance by presumably adenosylcobalamin at 525 nm
-
?
ATP + cob(I)alamine
triphosphate + adenosylcob(I)alamine
-
-
-
?
ATP + cob(I)yrinic acid a,c-diamide
triphosphate + adenosylcob(III)yrinic acid a,c-diamide
-
-
-
?
ATP + cob(II)alamin
triphosphate + adenosylcob(II)alamine
ATP + cob(II)alamine
triphosphate + adenosylcob(II)alamine
-
-
-
?
ATP + cob(II)inamide
triphosphate + adenosylcob(II)inamide
-
-
-
?
ATP + cobalamin
triphosphate + adenosylcob(III)alamin
-
enzyme is absolutely specific for ATP or dATP as adenosyl donors, ATP is the preferred adenosyl donor
-
-
?
ATP + cobalamin
triphosphate + adenosylcobalamin
enzyme is absolutely specific for ATP or dATP as adenosyl donors
-
-
ir
ATP + cobinamide
triphosphate + adenosylcobinamide
ATP + hydroxocobalamin
?
-
-
-
?
ATP + hydroxycobalamin
adenosylcobalamin + phosphate + diphosphate
37°C, pH 8, 0.5 mM ATP, 0.05 mM hydroxycobalamin, in presence of 1 mM titanium(III)citrate
measured by decrease in absorbance at 388 nm
-
?
ATP + hydroxycobalamin
tripolyphosphate + adenosylcobalamin + H2O
-
coenzyme B12 synthesis from vitamin B12, dimethylbenzimidazole arm of vitamin B12 plays no role in substrate positioning, corrinoid adenosylation assay: anaerobic, pH 6, 25°C, 1 or 2 mM FMN, 10 or 20 mM NADH, NAD(P)H: flavin oxidoreductase, 2 h incubation for complete reduction of hydroxycobalamin to cob(II)alamin before initiation of adenosyltransfer
measuring difference in absorbance by adenosylcobalamin at 525 nm
-
?
cob(I)alamin + ADP
adenosylcobalamin + diphosphate
cob(I)alamin + ATP
adenosylcobalamin + ?
-
in the co+ assay the cobalt ion of cobalamin is chemically reduced in solution to cob(I)alamin by Ti(III)citrate, allowing the cob(I)alamin adenosylation reaction to be measured directly. The Co+ assay is performed under anoxic conditions
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
cob(I)alamin + ATP + H2O + H+
adenosylcobalamin + diphosphate + phosphate
cob(I)alamin + CTP + H2O + H+
cytosylcobalamin + diphosphate + phosphate
-
-
-
-
?
cob(I)alamin + dATP + H2O + H+
deoxyadenosylcobalamin + diphosphate + phosphate
-
-
-
-
?
cob(I)alamin + GTP + H2O + H+
guanosylcobalamin + diphosphate + phosphate
-
low activity
-
-
?
cob(I)alamin + ITP
hypoxanthosylcobalamin + diphosphate + phosphate
-
low activity
-
-
?
cob(I)alamin + UTP
uranylcobalamin + diphosphate + phosphate
-
low activity
-
-
?
cob(I)inamide + ATP
5'-deoxy-5'-adenosyl-cob(I)inamide + polyphosphate
-
-
?
cob(I)inamide + ATP
adenosylcobinamide + triphosphate
cob(I)yric acid + ATP
5'-deoxy-5'-adenosyl-cob(I)yric acid + polyphosphate
-
-
?
cob(I)yrinic acid a,c-diamide + ATP
5'-deoxy-5'-adenosyl-cob(I)yrinic acid a,c-diamide + polyphosphate
-
-
?
cob(II)alamin
cob(I)alamin
G97, T161, and H183 possible role in stabilizing four-coordinate, cob(II)alamin C-terminal His-tagged enzyme binds cob(II)alamin base-off while N-terminal His-tagged enzyme binds it base-on (impaired base-off transition), only mutants S68F, K78Q, K78R, R186W, and R190C also bind cob(II)alamin base-off
-
-
?
cob(II)alamin + ATP
adenosylcobalamin + ?
-
in the Co2+ assay the NADPH-dependent flavodoxin protein reductase/flavodoxin system is used to reduce Co2+ to Co+. In this Co2+ assay, the PduO enzyme must bind cob(II)alamin and facilitate the generation of cob(I)alamin in its active site
-
-
?
CTP + cob(I)alamin
triphosphate + cytosylcobalamin
-
polymorphic variants 239K and 239M, 9% activity compared to ATP with enzyme variant 239K, 6% activity compared to ATP with enzyme variant 239M
-
-
?
CTP + cob(I)alamin + H2O
cytidylcobalamin + diphosphate + phosphate
-
37°C
-
-
?
cyanocob(I)alamin + ATP
tripolyphosphate + alpha-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide
dATP + cob(I)alamin
tripolyphosphate + deoxyadenosylcobalamin
-
-
?
dATP + cobalamin
triphosphate + deoxyadenosylcob(III)alamin
-
enzyme is absolutely specific for ATP or dATP as adenosyl donors, dATP results in 21% of the activity with ATP
-
-
?
dATP + cobalamin
triphosphate + deoxyadenosylcobalamin
enzyme is absolutely specific for ATP or dATP as adenosyl donors
-
-
ir
GTP + cob(I)alamin
triphosphate + guanosylcobalamin
-
polymorphic variants 239K and 239M, 16% activity compared to ATP with enzyme variant 239K, 14% activity compared to ATP with enzyme variant 239M
-
-
?
GTP + cob(I)alamin + H2O
guanosylcobalamin + diphosphate + phosphate
-
37°C
-
-
?
ITP + cob(I)alamin + H2O
inosylcobalamin + diphosphate + phosphate
-
37°C
-
-
?
UTP + cob(I)alamin
triphosphate + uridylcobalamin
-
polymorphic variants 239K and 239M, 8% activity compared to ATP with enzyme variant 239K, 6% activity compared to ATP with enzyme variant 239M
-
-
?
UTP + cob(I)alamin + H2O
uridylcobalamin + diphosphate + phosphate
-
37°C
-
-
?
additional information
?
-
2 ATP + 2 cob(II)alamin + a reduced flavoprotein
2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
-
-
-
?
2 ATP + 2 cob(II)alamin + a reduced flavoprotein
2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
-
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(I)alamine
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(I)alamine
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(I)alamine
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
-
adenosyltransferase enzymes lower the thermodynamic barrier of the Co2+ toCo+ reduction needed for the formation of the unique organometalic Co-C bond of adenosylcobalamin
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
reaction mechanism: assimilated cobalamin is reduced to co(II)alamin, that then binds to the enzyme-ATP complex, further reduction yields a nucleophilic four coordinated Co1+ intermediate that attacks the 5'-carbon of the cosubstrate ATP to generate adenosylcobalamin and triphosphate, spectroscopic analysis, enzyme-induced base-on/base-off conversion activating the cobalamin substrate for reduction
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
-
adenosyltransferase enzymes lower the thermodynamic barrier of the Co2+ to Co+ reduction needed for the formation of the unique organometalic Co-C bond of adenosylcobalamin
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
binding of the substrate ATP to ATR that is fully loaded with 5'-deoxyadenosylcobalamin leads to the ejection of 1 equivalent of the cofactor into solution. In the presence of methylmalonyl-CoA mutase and ATP, 5'-deoxyadenosylcobalamin is transferred from ATR to the acceptor protein in a process that exhibits an 3.5fold lower Kact for ATP compared to the one in which cofactor is released into solution. ATP favorably influences cofactor transfer in the forward direction by reducing the ratio of apo-methylmalonyl-CoA mutase/holo-ATR required for delivery of 1 equivalent of 5'-deoxyadenosylcobalamin, from 4 to 1. A rotary rotary mechanism for ATR function is proposed in which, at any given time, only two of its active sites are used for 5'-deoxyadenosylcobalamin synthesis and where binding of ATP to the vacant site leads to the transfer of the high value 5'-deoxyadenosylcobalamin product to the acceptor mutase
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
final step in the conversion of vitamin B12 to coenzyme B12, the latter being required for degradation of 1,2-propanediol
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
last step in the corrinoid adenosylation pathway, EutT and CobA
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
mechanism of adenosylcobalamin biosynthesis
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
CobA has an ATP-binding P-loop motif, while EutT has a cysteine-rich region reminiscent of a conserved S-adenosylmethionine Fe-S cluster motif
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
formation of the the essential C-Co bond by transferring the adenosyl group from a molecule of ATP to a transient Co1+ corrinoid species generated by the active site
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
last step in the corrinoid adenosylation pathway, EutT and CobA
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
CobA has an ATP-binding P-loop motif, while EutT has a cysteine-rich region reminiscent of a conserved S-adenosylmethionine Fe-S cluster motif
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcobalamin
-
polymorphic variants 239K and 239M, biosynthesis of adenosylcobalamin
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcobalamin
-
polymorphic variants 239K and 239M, ATP is highly preferred as adenosyl donor
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcobalamin
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
r
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
stereospecific process which proceeds with overall inversion of configuration at C-5' of the adenosyl moiety
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
transfers the adenosyl-group of ATP to the reduced cobalt atom of the cobalamin molecule
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
involved in vitamin B12 metabolism
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
the main role of this enzyme is apparently the conversion of inactive cobalamins to adenosyl cobalamin for 1,2 propanediol degradation
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
tripolyphosphate + coenzyme B12
-
-
-
?
ATP + cob(I)alamin
tripolyphosphate + coenzyme B12
-
-
-
?
ATP + cob(II)alamin
triphosphate + adenosylcob(II)alamine
-
-
-
-
?
ATP + cob(II)alamin
triphosphate + adenosylcob(II)alamine
-
-
-
-
?
ATP + cobinamide
triphosphate + adenosylcobinamide
-
-
-
-
?
ATP + cobinamide
triphosphate + adenosylcobinamide
-
-
-
?
cob(I)alamin + ADP
adenosylcobalamin + diphosphate
-
-
-
-
?
cob(I)alamin + ADP
adenosylcobalamin + diphosphate
-
-
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
-
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
adenosylcobalamin is a cofactor required by the methylmalonyl-CoA mutase
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
cobalamin assimilation and recycling pathway, overview, enzyme deficiency causes methylmalonic aciduria, MMA, is an autosomal recessive disease with symptoms that include ketoacidosis, lethargy, recurrent vomiting, dehydration, respiratory distress, muscular hypotonia and death due to methylmalonic acid levels that are up to 1000fold greater than normal, overview
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
dissociation constant (Kd) of wild-type MMAB for hydroxomethylcobalamin is 0.051 mM and for ATP is 0.365 mM, cobalamin enhances the affinity of MMAB for ATP, while ATP does not show detectable effects on cobalamin binding
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
adenosylation of the corrinoid ring of cob(I)alamin generates coenzyme B12, i.e. adenosylcobalamin or AdoCbl, an essential cofactor used by enzymes that catalyze intramolecular rearrangements, deaminations, dehydrations, reductions, and reductive dehalogenations
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
adenosylation of the corrinoid ring of cob(I)alamin, active site structure, ATP binding motif at the protein N terminus
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
upon binding to LrPduO that is preincubated with ATP, both Co2+corrinoids undergo a partial (40-50%) conversion to distinct paramagnetic Co2+ species. The spectroscopic signatures of these species are consistent with essentially four-coordinate, square-planar Co2+ complexes. For effecting Co2+ to Co1+ reduction the formation of an activated Co2+ corrinoid intermediate that lacks any significant axial bonding interactions is involved to stabilize the redoxactive, Co 3dz2-based molecular orbital
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
adenosylation of the corrinoid ring of cob(I)alamin generates coenzyme B12, i.e. adenosylcobalamin or AdoCbl, an essential cofactor used by enzymes that catalyze intramolecular rearrangements, deaminations, dehydrations, reductions, and reductive dehalogenations
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
adenosylation of the corrinoid ring of cob(I)alamin, active site structure, ATP binding motif at the protein N terminus
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
-
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
cobalamin is a better substrate than cobinamide, the beta-phosphate of ATP is required for binding to the enzyme
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
the enzyme is required to adenosylate de novo biosynthetic intermediates of adenosylcobalamin and to salvage incomplete and complete corrinoids from the environment of this bacterium
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
in vitro reduced flavodoxin provides an electron to generate the co(I)rrinoid substrate in the CobA active site, modeling of enzyme ligand interaction, residues R9 and R165 are important for CobA-FldA docking but not to catalysis, overview
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cob(I)alamin + ATP + H2O + H+
adenosylcobalamin + diphosphate + phosphate
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cob(I)alamin + ATP + H2O + H+
adenosylcobalamin + diphosphate + phosphate
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FMN and NADH are used to reduce cob(III)alamin to cob(I)alamin, the enzyme shows ATP hydrolyzing activity to adenosine and triphosphate in absence of cob(I)alamin
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cob(I)inamide + ATP
adenosylcobinamide + triphosphate
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upon binding to LrPduO that is preincubated with ATP, both Co2+corrinoids undergo a partial (40-50%) conversion to distinct paramagnetic Co2+ species. The spectroscopic signatures of these species are consistent with essentially four-coordinate, square-planar Co2+ complexes. For effecting Co2+ to Co1+ reduction the formation of an activated Co2+ corrinoid intermediate that lacks any significant axial bonding interactions is involved to stabilize the redoxactive, Co 3dz2-based molecular orbital
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cob(I)inamide + ATP
adenosylcobinamide + triphosphate
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cob(I)inamide + ATP
adenosylcobinamide + triphosphate
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cobalamin is a better substrate than cobinamide, the beta-phosphate of ATP is required for binding to the enzyme
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cyanocob(I)alamin + ATP
tripolyphosphate + alpha-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide
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cyanocob(I)alamin + ATP
tripolyphosphate + alpha-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide
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additional information
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ATP:Cobalamin adenosyltransferases catalyze the transfer a 5'-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B12
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additional information
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MgATP and Cob(II)alamin binding sites, structure comparison overview
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additional information
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additional information
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additional information
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UTP, GTP, ITP are poor substrates
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additional information
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S-adenosylmethionine, vitamin B12r or B12a, AMP, ADP are no substrates
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additional information
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S-adenosylmethionine, vitamin B12r or B12a, AMP, ADP are no substrates
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additional information
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hydroxocobamides or cyanocobamides in which benzimidazole replaces 5,6-dimethylbenzimidazole, or cyanocobamide in which an adenine group replaces 5,6-dimethylbenzimidazole, can also act as substrates
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additional information
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the enzyme interacts with the methionine synthase reductase MSR, which catalyzes the reduction of cob(II)almin to cob(I)alamin, both enzymes activate each other, stoichiometry of the MSR-ATR system, overview
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additional information
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no activity with ADP and AMP
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additional information
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enzyme defects cause methylmalonic aciduria type B, regulation, overview
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additional information
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the enzyme catalyzes the final step in the conversion of cyanocobalamin, i.e. vitamin B12, to the essential human cofactor adenosylcobalamin, defects in the enzyme through mutations in the gene encoding the enzyme can result in the metabolic disorder known as methylmalonic aciduria, MMA
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additional information
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the enzyme catalyzes the final step in the conversion of cyanocobalamin, i.e. vitamin B12, to the essential human cofactor adenosylcobalamin, defects in the enzyme through mutations in the gene encoding the enzyme can result in the metabolic disorder known as methylmalonic aciduria, MMA
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2.5.1.17 corrinoid adenosyltransferase
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