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Co2+
can substitute for Zn2+
Fe2+
anaerobic reconstitution of apoenzyme with Fe2+, which yields an enzyme with an effective kcat that exceeds that for the Zn2+-reconstituted enzyme. The Fe2+-reconstituted enzyme contains high spin Fe2+ that, when oxidized to Fe3+, inactivates the enzyme. Reconstitution with Fe3+ is unsuccessful
Cd2+
-
replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme
Zinc
-
contains 1 Zn per subunit
Zn2+
zinc enzyme
Zn2+
zinc-containing enzyme
Zn2+
the enzyme contains contains catalytic zinc
Co2+
-
isomorphously replaces zinc
Co2+
-
activates to a 2fold activity compared to the activity with Zn2+
Fe2+
-
contains one iron ion per monomer when synthesized in Methanosarcina acetivorans
Fe2+
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme. The Fe2+-reconstituted enzyme contains high spin Fe2+ that, when oxidized to Fe3+, inactivates the enzyme. Reconstitution with Fe3+ is unsuccessful
Fe2+
the homotrimer purified from Escherichia coli cultured with supplemental zinc contains 0.71 zinc and 0.15 iron per monomer. Enzyme purified from Escheria coli cultured with supplemental iron contains 0.15 iron per monomer and only a trace amount of zinc
Fe2+
-
when overproduced in Escherichia coli or in Methanosarcina acetivorans and subsequently anaerobically purified, the enzyme contains Fe2+ in the active site and is 4fold more active. In these conditions, catalytic activity is rapidly lost after exposure to air, as a consequence of the oxidation of Fe2+ to Fe3+ and loss of the metal from the active site, thus convincing evidence is that iron is the physiologically relevant metal for this enzyme
Zn2+
-
-
Zn2+
-
contains one zinc ion per monomer when overproduced in Escherichia coli
Zn2+
-
required for activity. Replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme
Zn2+
the homotrimer purified from Escherichia coli cultured with supplemental zinc contains 0.71 zinc and 0.15 iron per monomer. Enzyme purified from Escherichia coli cultured with supplemental iron contains 0.15 iron per monomer and only a trace amount of zinc
Zn2+
-
the individual subunits are only weakly folded and fractionally associated in the absence of Zn2+. The crucial thermodynamic step in the assembly of the trimeric holo-Cam is the incorporation of the three Zn2+ ions, events which must occur after the monomer is resident on the surface and has access to other monomers
Zn2+
-
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
additional information
-
reconstitution of the apoenzyme with Cu2+, Mn2+, Ni2+, or Cd2+ yields enzymes with effective kcat values that are 10% or less than the value for the Zn2+-reconstituted apoenzyme
additional information
reconstitution of the apoenzyme with Cu2+, Mn2+, Ni2+, or Cd2+ yields enzymes with effective kcat values that are 10% or less than the value for the Zn2+-reconstituted apoenzyme
additional information
-
the metal ion in the enzyme isolated directly from Methanosarcina thermophila is not been determined since only enzyme overproduced in Escherichia coli is characterized
additional information
the metal ion in the enzyme isolated directly from Methanosarcina thermophila is not been determined since only enzyme overproduced in Escherichia coli is characterized
additional information
-
analysis of three-dimensional structures of MtCam, in both Zn- and Co-bound forms, overview. Structure comparisons
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1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
-
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
-
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
-
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
-
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
-
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme gammaCA
3-[amino(dihydroxy)-lambda4-sulfanyl]aniline
-
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme gammaCA, i.e. daranide
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
-
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme gammaCA
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme gammaCA
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme gammaCA
CN-
best anion inhibitors for Zn2+-substituted enzyme are cyanate and hydrogen sulfide
HS-
best anion inhibitors for Zn2+-substituted enzyme are cyanate and hydrogen sulfide
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme gammaCA
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
-
azide
weak inhibitor of the Zn(II)-substituted enzyme
Carbonate
weak inhibitor of the Zn(II)-substituted enzyme, best inhibitor of the Co(II)-substituted enzyme
Cyanate
best inhibitor of the Zn(II)-substituted enzyme
hydrogen sulfide
best inhibitor of the Zn(II)-substituted enzyme
hydrogen sulfite
weak inhibitor of the Zn(II)-substituted enzyme
hydrogencarbonate
good inhibitor of the Co(II)-substituted enzyme
nitrate
good inhibitor of the Co(II)-substituted enzyme
nitrite
weak inhibitor of the Zn(II)-substituted enzyme
thiocyanate
weak inhibitor of the Zn(II)-substituted enzyme
Zn2+
-
the enzyme binds three catalytic Zn2+ ions at symmetry-related subunit interfaces. Zinc binding drives the folding and association of the homotrimeric enzyme
acetazolamide
-
acetazolamide
IC50: 0.4 mM
acetazolamide
isoenzyme gammaCA
ethoxzolamide
-
ethoxzolamide
isoenzyme gammaCA
sulfanilamide
-
topiramate
-
topiramate
isoenzyme gammaCA
additional information
-
fluoride, chloride, and sulfate do not inhibit the Zn2+-substituted enzyme and the Co2+-substituted enzyme appreciably
-
additional information
fluoride, chloride, and sulfate do not inhibit the Zn2+-substituted enzyme and the Co2+-substituted enzyme appreciably
-
additional information
-
Zn(II)- and Co(II)-substituted enzymes show a very different behavior against anion inhibitors.The best Zn-Cam anion inhibitors are hydrogen sulfide and cyanate whereas thiocyanate, azide, carbonate, nitrite, and hydrogensulfite are weaker inhibitors. The inhibition of the Zn(II)-substituted enzyme by sulfide is puzzling since Cam is proposed to be located outside the cytoplasmic membrane where it is exposed to high levels of sulfide in the anaerobic environments. The best inhibitors of the Co(II)-substituted enzyme is carbonate, followed by nitrate and hydrogencarbonate. Fluoride, chloride, and sulfate do not inhibit either Zn(II)- or Co(II)-substituted enzyme appreciably up to concentrations of 200 mM. This lack of inhibition may represent an adaptation to marine environments high in chloride and sulfate
-
additional information
Zn(II)- and Co(II)-substituted enzymes show a very different behavior against anion inhibitors.The best Zn-Cam anion inhibitors are hydrogen sulfide and cyanate whereas thiocyanate, azide, carbonate, nitrite, and hydrogensulfite are weaker inhibitors. The inhibition of the Zn(II)-substituted enzyme by sulfide is puzzling since Cam is proposed to be located outside the cytoplasmic membrane where it is exposed to high levels of sulfide in the anaerobic environments. The best inhibitors of the Co(II)-substituted enzyme is carbonate, followed by nitrate and hydrogencarbonate. Fluoride, chloride, and sulfate do not inhibit either Zn(II)- or Co(II)-substituted enzyme appreciably up to concentrations of 200 mM. This lack of inhibition may represent an adaptation to marine environments high in chloride and sulfate
-
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additional information
additional information
-
6.09
CO2
pH 7.5, 37°C, variant R59H, 100 mM guanidine hydrochloride
6.5
CO2
pH 7.5, 37°C, variant R59C, 100 mM ethylguanidine
9.45
CO2
pH 7.5, 37°C, variant R59A, 100 mM aminoguanidine
11.7
CO2
pH 7.5, 37°C, variant R59A, 150 mM guanidine
12.2
CO2
pH 7.5, 37°C, variant R59A, 100 mM methylguanidine
12.8
CO2
pH 7.5, 37°C, variant R59A, 100 mM 1.3-diaminoguanidine
13.6
CO2
pH 7.5, 37°C, variant R59C, 100 mM guanidine
14.5
CO2
pH 7.5, 37°C, variant R59A, 50 mM guanidine
15.7
CO2
pH 7.5, 37°C, variant R59A
16.2
CO2
pH 7.5, 37°C, variant R59A, 100 mM ethylguanidine
16.3
CO2
pH 7.5, 37°C, variant R59K, 100 mM guanidine hydrochloride
16.7
CO2
pH 7.5, 37°C, 100 mM guanidine hydrochloride
17.1
CO2
pH 7.5, 37°C, variant R59A, 100 mM guanidine
17.3
CO2
pH 7.5, 37°C, variant R59C, 100 mM methylguanidine, variant R59Q, 100 mM guanidine hydrochloride
19.1
CO2
pH 7.5, 37°C, variant R59K, 100 mM guanidine hydrochloride
19.3
CO2
pH 7.5, 37°C, variant R59E, 100 mM guanidine hydrochloride
21.8
CO2
pH 7.5, 37°C, wild-type, without guanidine hydrochloride
25
CO2
pH 7.5, 37°C, variant R59H, without guanidine hydrochloride
25.4
CO2
pH 7.5, 37°C, variant R59A, 100 mM ethylamine
26.2
CO2
pH 7.5, 37°C, variant R59A, 100 mM urea
33.4
CO2
pH 7.5, 37°C, variant R59K, without guanidine hydrochloride
33.9
CO2
pH 7.5, 37°C, variant R59Q, without guanidine hydrochloride
34
CO2
pH 7.5, 37°C, variant R59A, 100 mM imidazole
34.2
CO2
pH 7.5, 37°C, variant R59C
43.3
CO2
pH 7.5, 37°C, variant R59M, without guanidine hydrochloride
47.6
CO2
pH 7.5, 37°C, variant R59C, 100 mM aminoguanidine
51.4
CO2
pH 7.5, 37°C, variant R59E, without guanidine hydrochloride
0.8
CO2
-
pH 7.5, 25°C, variant E84A, 50 mM MOPS-Ac buffer
1.1
CO2
-
pH 7.5, 25°C, variant E84C, 50 mM MOPS buffer
1.2
CO2
-
pH 7.5, 25°C, variant E84Q, 50 mM MOPS buffer
1.4
CO2
-
pH 7.5, 25°C, variant E62Q, 50 mM MOPS buffer
1.5
CO2
-
pH 7.5, 25°C, variant E84A and E84K, 50 mM MOPS buffer
2.1
CO2
-
pH 7.5, 25°C, variant E84S and E84Y, 50 mM MOPS buffer
2.5
CO2
-
pH 7.5, 25°C, variant E62T, 50 mM MOPS buffer
2.9
CO2
-
pH 7.5, 25°C, variant E62A/E84A, 50 mM MOPS buffer
3
CO2
-
pH 7.5, 25°C, variant E62Y, 50 mM MOPS buffer
3
CO2
pH 7.5, 25°C, enzyme cultured with supplemental iron
3.1
CO2
pH 7.5, 25°C, enzyme cultured with supplemental zinc
3.2
CO2
-
pH 7.5, 25°C, variant E84H, 50 mM MOPS buffer
3.8
CO2
-
pH 7.5, 25°C, variant E62C, 50 mM MOPS buffer
5.4
CO2
-
pH 7.5, 25°C, variant E62D/E84D, 50 mM MOPS buffer
5.5
CO2
-
pH 7.5, 25°C, variant E62A, 50 mM MOPS-Ac buffer
6.5
CO2
-
pH 7.5, 25°C, variant E62A, 50 mM MOPS buffer
7.6
CO2
-
pH 7.5, 25°C, variant E62H, 50 mM MOPS buffer
8.8
CO2
-
pH 7.5, 25°C, variant E84A, 50 mM IMID buffer
9.4
CO2
-
pH 7.5, 25°C, variant E62A, 50 mM IMID buffer
12.6
CO2
-
pH 8.5, 25°C, wild-type, D2O
14.7
CO2
-
pH 7.5, 25°C, wild-type, D2O
16.9
CO2
-
pH 7.5, 25°C, variant E88A, 50 mM MOPS buffer
18.1
CO2
-
pH 7.5, 25°C, variant E84D, 50 mM MOPS buffer
18.8
CO2
-
pH 7.5, 25°C, variant E62D, 50 mM MOPS buffer
19.3
CO2
-
pH 7.5, 25°C, variant E89A, 50 mM MOPS buffer
20
CO2
-
pH 8.5, 25°C, wild-type, H2O
22.5
CO2
-
pH 7.5, 25°C, wild-type, 50 mM MOPS-Ac buffer
23.8
CO2
-
pH 6.5, 25°C, wild-type, D2O
27.8
CO2
-
pH 7.5, 25°C, wild-type, 50 mM MOPS buffer
28.5
CO2
-
pH 6.5, 25°C, wild-type
44.1
CO2
-
pH 7.5, 25°C, wild-type, 50 mM IMID buffer
additional information
additional information
-
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
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additional information
additional information
-
2 - 8
CO2
pH 7.5, 37°C, variant R59A, 100 mM urea
10
CO2
pH 7.5, 37°C, variant R59Q, without guanidine hydrochloride
12
CO2
pH 7.5, 37°C, variant R59A, 100 mM 1.3-diaminoguanidine, variant R59H plus 100 mM guanidine hydrochloride
13
CO2
pH 7.5, 37°C, variant R59M, without guanidine hydrochloride
42
CO2
pH 7.5, 37°C, variant R59H, without guanidine hydrochloride
67
CO2
pH 7.5, 37°C, variant R59E, without guanidine hydrochloride
70
CO2
pH 7.5, 37°C, variant R59A
110
CO2
pH 7.5, 37°C, variant R59A, 100 mM imidazole
159
CO2
pH 7.5, 37°C, variant R59M, 100 mM guanidine hydrochloride
160
CO2
pH 7.5, 37°C, variant R59A, 100 mM ethylamine
310
CO2
pH 7.5, 37°C, variant R59C, 100 mM ethylguanidine
320
CO2
pH 7.5, 37°C, variant R59C, 100 mM aminoguanidine
350
CO2
pH 7.5, 37°C, variant R59A, 100 mM aminoguanidine
520
CO2
pH 7.5, 37°C, variant R59C
627
CO2
pH 7.5, 37°C, variant R59Q, 100 mM guanidine hydrochloride
990
CO2
pH 7.5, 37°C, variant R59C, 100 mM methylguanidine
2170
CO2
pH 7.5, 37°C, variant R59C, 100 mM guanidine
2250
CO2
pH 7.5, 37°C, variant R59A, 150 mM guanidine
2700
CO2
pH 7.5, 37°C, variant R59A, 50 mM guanidine
2701
CO2
pH 7.5, 37°C, variant R59A, 50 mM guanidine
2740
CO2
pH 7.5, 37°C, variant R59K, 100 mM guanidine hydrochloride
3270
CO2
pH 7.5, 37°C, variant R59A, 100 mM guanidine
4720
CO2
pH 7.5, 37°C, variant R59K, without guanidine hydrochloride
5690
CO2
pH 7.5, 37°C, variant R59A, 100 mM methylguanidine
5800
CO2
25°C, pH 7.5, mutant enzyme W19N
6500
CO2
25°C, pH 7.5, mutant enzyme W19F
7140
CO2
pH 7.5, 37°C, variant R59A, 100 mM ethylguanidine
7900
CO2
25°C, pH 7.5, mutant enzyme W19A
20000
CO2
pH 7.5, 37°C, variant R59E, without guanidine hydrochloride
22900
CO2
pH 7.5, 37°C, wild-type, 100 mM guanidine hydrochloride
32400
CO2
25°C, pH 7.5, wild-type enzyme
62900
CO2
pH 7.5, 37°C, wild-type, without guanidine hydrochloride
79300
CO2
25°C, pH 7.5, mutant enzyme Y200S
95000
CO2
25°C, pH 7.5, mutant enzyme Y200A
120100
CO2
25°C, pH 7.5, mutant enzyme Y200F
0.000493
CO2
pH 7.5, 25°C, enzyme cultured with supplemental zinc
0.00061
CO2
-
pH 5.5-7.5, 25°C, Zn-Cam
0.00104
CO2
-
pH 5.5-7.5, 25°C, Co-Cam
0.0052
CO2
pH 7.5, 25°C, enzyme cultured with supplemental iron
47
CO2
-
pH 7.5, 25°C, variant E62Y, 50 mM MOPS buffer
210
CO2
-
pH 7.5, 25°C, variant E62A/E84A, 50 mM MOPS buffer
340
CO2
-
pH 7.5, 25°C, variant E62A, 50 mM MOPS-Ac buffer
410
CO2
-
pH 7.5, 25°C, variant E62Q, 50 mM MOPS buffer
510
CO2
-
pH 7.5, 25°C, variant E84Y, 50 mM MOPS buffer
720
CO2
-
pH 7.5, 25°C, variant E84C and E62A, 50 mM MOPS buffer
800
CO2
-
pH 7.5, 25°C, variant E84A, 50 mM MOPS-Ac buffer
860
CO2
-
pH 7.5, 25°C, variant E62T, 50 mM MOPS buffer
870
CO2
-
pH 7.5, 25°C, variant E84A, 50 mM MOPS buffer
910
CO2
-
pH 7.5, 25°C, variant E62C, 50 mM MOPS buffer
1050
CO2
-
pH 7.5, 25°C, variant E62H, 50 mM MOPS buffer
1070
CO2
-
pH 7.5, 25°C, variant E62A, 50 mM IMID buffer
1080
CO2
-
pH 7.5, 25°C, variant E84S, 50 mM MOPS buffer
1300
CO2
-
pH 7.5, 25°C, variant E84Q, 50 mM MOPS buffer
1900
CO2
-
pH 7.5, 25°C, variant E84K, 50 mM MOPS buffer
4700
CO2
-
pH 7.5, 25°C, variant E62D/E84D, 50 mM MOPS buffer
7100
CO2
-
pH 5.7-9.5, 25°C, wild-type
9300
CO2
-
pH 6.5, 25°C, wild-type, D2O
9500
CO2
-
pH 7.5, 25°C, variant E84H, 50 mM MOPS buffer
16700
CO2
-
pH 7.5, 25°C, wild-type, D2O
16800
CO2
-
pH 7.5, 25°C, variant E62D, 50 mM MOPS buffer
18600
CO2
-
pH 6.5, 25°C, wild-type
21000
CO2
-
pH 7.5, 25°C, variant E84D, 50 mM MOPS buffer
22600
CO2
-
pH 8.5, 25°C, wild-type, D2O
24700
CO2
-
pH 7.5, 25°C, wild-type, 50 mM MOPS-Ac buffer
26500
CO2
-
pH 7.5, 25°C, variant E88A, 50 mM MOPS buffer
29100
CO2
-
pH 7.5, 25°C, variant E89A, 50 mM MOPS buffer
35100
CO2
-
pH 7.5, 25°C, variant E84A, 50 mM IMID buffer
56800
CO2
-
pH 7.5, 25°C, wild-type, 50 mM MOPS buffer
58900
CO2
-
pH 8.5, 25°C, wild-type
71900
CO2
-
pH 7.5, 25°C, wild-type, 50 mM IMID buffer
68000
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and aerobically purified
231000
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Methanosarcina acetivorans and anaerobically purified
243000
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and anaerobically purified
additional information
additional information
-
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
-
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
additional information
additional information
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
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additional information
additional information
-
400
CO2
25°C, pH 7.5, mutant enzyme W19F
600
CO2
25°C, pH 8.8, mutant enzyme W19F
630
CO2
25°C, pH 7.5, mutant enzyme W19N
790
CO2
25°C, pH 7.5, mutant enzyme W19A
1300
CO2
25°C, pH 8.8, mutant enzyme W19N
1400
CO2
25°C, pH 8.8, mutant enzyme W19A
2000
CO2
25°C, pH 7.5, wild-type enzyme
3100
CO2
25°C, pH 8.8, wild-type enzyme
5900
CO2
25°C, pH 7.5, mutant enzyme Y200S
7000
CO2
25°C, pH 7.5, mutant enzyme Y200A
7100
CO2
25°C, pH 7.5, mutant enzyme Y200F
7900
CO2
25°C, pH 8.8, mutant enzyme Y200F
10200
CO2
25°C, pH 8.8, mutant enzyme Y200S
10300
CO2
25°C, pH 8.8, mutant enzyme Y200A
0.00016
CO2
pH 7.5, 25°C, enzyme cultured with supplemental zinc
0.0017
CO2
pH 7.5, 25°C, enzyme cultured with supplemental iron
3100
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and aerobically purified
3900
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Methanosarcina acetivorans and anaerobically purified
5400
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and anaerobically purified
additional information
additional information
-
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
-
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
additional information
additional information
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
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0.00015 - 0.00019
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
0.00027 - 0.0013
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
0.00035 - 0.0085
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
0.00083 - 0.00095
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
0.00012 - 0.00061
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
0.00046
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme gammaCA
0.00017 - 0.00124
3-[amino(dihydroxy)-lambda4-sulfanyl]aniline
0.00019
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme gammaCA, i.e. daranide
0.00018 - 0.00636
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
0.00028 - 0.00172
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
0.00014 - 0.00074
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
0.00097 - 0.0042
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
0.00028 - 0.00066
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
0.00012
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme gammaCA
0.00041
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme gammaCA
0.00083
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme gammaCA
0.000063 - 0.00143
acetazolamide
0.00014 - 0.00101
celecoxib
0.00041 - 0.00171
dorzolamide
0.0002 - 0.00074
ethoxzolamide
0.00014 - 0.00017
methazolamide
0.00014
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme gammaCA
0.000096 - 0.00336
sulfamic acid
0.00596 - 0.069
sulfamide
0.00025 - 0.00393
sulfanilamide
0.00012 - 0.00102
topiramate
0.00013 - 0.00024
valdecoxib
0.00022 - 0.0022
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
0.05 - 2
hydrogen sulfide
1.8 - 11.7
hydrogen sulfite
0.1 - 42
hydrogencarbonate
0.00015
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00019
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00027
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.0013
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00035
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.0085
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00083
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00095
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00012
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00061
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00017
3-[amino(dihydroxy)-lambda4-sulfanyl]aniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00124
3-[amino(dihydroxy)-lambda4-sulfanyl]aniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00018
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00636
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00028
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00172
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00014
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00074
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00097
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.0042
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00028
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00066
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.000063
acetazolamide
isoenzyme gammaCA
0.000063
acetazolamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00143
acetazolamide
20°C, pH not specified in the publication, Co2+-containing enzyme
22.2
Br-
20°C, pH not specified in the publication, Co2+-substituted enzyme
160
Br-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.00014
celecoxib
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00101
celecoxib
20°C, pH not specified in the publication, Co2+-containing enzyme
0.68
CN-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
51.5
CN-
20°C, pH not specified in the publication, Co2+-substituted enzyme
0.09
CNO-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
4.7
CNO-
20°C, pH not specified in the publication, Co2+-substituted enzyme
0.009
CO32-
20°C, pH not specified in the publication, Co2+-substituted enzyme
6.7
CO32-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.00041
dorzolamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00171
dorzolamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0002
ethoxzolamide
isoenzyme gammaCA
0.0002
ethoxzolamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00074
ethoxzolamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.1
HCO3-
20°C, pH not specified in the publication, Co2+-substituted enzyme
42
HCO3-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.05
HS-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
2
HS-
20°C, pH not specified in the publication, Co2+-substituted enzyme
1.8
HSO3-
20°C, pH not specified in the publication, Co2+-substituted enzyme
11.7
HSO3-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
5.3
I-
20°C, pH not specified in the publication, Co2+-substituted enzyme
160
I-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.00014
methazolamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00017
methazolamide
20°C, pH not specified in the publication, Co2+-containing enzyme
4.9
N3-
20°C, pH not specified in the publication, Co2+-substituted enzyme
5.8
N3-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
6.8
NO2-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
7.3
NO2-
20°C, pH not specified in the publication, Co2+-substituted enzyme
0.09
NO3-
20°C, pH not specified in the publication, Co2+-substituted enzyme
36.5
NO3-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
6.1
SCN-
20°C, pH not specified in the publication, Co2+-substituted enzyme
7
SCN-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.000096
sulfamic acid
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00336
sulfamic acid
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00596
sulfamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.069
sulfamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00025
sulfanilamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00393
sulfanilamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00012
topiramate
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00102
topiramate
isoenzyme gammaCA
0.00102
topiramate
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00013
valdecoxib
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00024
valdecoxib
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00022
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0022
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
20°C, pH not specified in the publication, Zn2+-containing enzyme
4.9
azide
Co(II)-substituted enzyme, pH and temperature not specified in the publication
5.8
azide
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
22.2
Br-
Co(II)-substituted enzyme, pH and temperature not specified in the publication
160
Br-
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.009
Carbonate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
6.7
Carbonate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.09
Cyanate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
4.7
Cyanate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
0.68
cyanide
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
51.5
cyanide
Co(II)-substituted enzyme, pH and temperature not specified in the publication
0.05
hydrogen sulfide
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
2
hydrogen sulfide
Co(II)-substituted enzyme, pH and temperature not specified in the publication
1.8
hydrogen sulfite
Co(II)-substituted enzyme, pH and temperature not specified in the publication
11.7
hydrogen sulfite
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.1
hydrogencarbonate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
42
hydrogencarbonate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
5.3
I-
Co(II)-substituted enzyme, pH and temperature not specified in the publication
160
I-
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.09
nitrate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
36.5
nitrate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
6.8
nitrite
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
7.3
nitrite
Co(II)-substituted enzyme, pH and temperature not specified in the publication
6.1
thiocyanate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
7
thiocyanate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
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R59A
site-directed mutagenesis
R59C
site-directed mutagenesis
R59E
site-directed mutagenesis
R59H
site-directed mutagenesis
R59K
site-directed mutagenesis
R59M
site-directed mutagenesis
R59Q
site-directed mutagenesis
W19A
kcat/km at pH 7.5 is 2.5fold lower than wild-type value, kcat/km at pH 8.8 is 2.2fold lower than wild-type value
W19F
kcat/km at pH 7.5 is 5fold lower than wild-type value, kcat/km at pH 8.8 is 5.2fold lower than wild-type value
W19N
kcat/km at pH 7.5 is 3.2fold lower than wild-type value, kcat/km at pH 8.8 is 2.4fold lower than wild-type value
Y200A
kcat/km at pH 7.5 is 3.5fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value
Y200F
kcat/km at pH 7.5 is 3.6fold higher than wild-type value, kcat/km at pH 8.8 is 2.5fold lower than wild-type value
Y200S
kcat/km at pH 7.5 is 3fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value
C148S
-
the mutation eliminate potential problems with the oxidation of the single cysteine residue at position 148
E62A
-
site-directed mutagenesis, large decrease in kcat
E62A/E84A
-
site-directed mutagenesis, large decrease in kcat
E62C
-
site-directed mutagenesis, large decrease in kcat
E62D
-
site-directed mutagenesis, 3fold decrease in kcat
E62D/E84D
-
site-directed mutagenesis, large decrease in kcat
E62H
-
site-directed mutagenesis, large decrease in kcat
E62Q
-
site-directed mutagenesis, large decrease in kcat
E62T
-
site-directed mutagenesis, large decrease in kcat
E62Y
-
site-directed mutagenesis, large decrease in kcat
E84 A
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 C
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 D
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 H
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 K
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 Q
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 S
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 Y
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84A
-
proton shuttle replaced with a residue that does not transfer protons
E88A
-
site-directed mutagenesis, large decrease in kcat
E89A
-
site-directed mutagenesis, large decrease in kcat
additional information
although Trp19 and Y200 are non-essential, they contribute to an extended active-site structure distant from the catalytic metal that fine tunes catalysis. Trp19 is important for both CO2/bicarbonate interconversion, and the proton transfer step of catalysis
additional information
-
although Trp19 and Y200 are non-essential, they contribute to an extended active-site structure distant from the catalytic metal that fine tunes catalysis. Trp19 is important for both CO2/bicarbonate interconversion, and the proton transfer step of catalysis
additional information
-
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview. Immobilizing the enzyme within solid supports improves the method. Formation of gamma-CA nanoassemblies, where individual enzymes are connected to each other and make multiple linked interactions with the reactor surface. This can be achieved by mutating specific enzyme residues to cysteines, in order to introduce sites for biotinylation, thus allowing the subsequent formation of stable nanostructures by cross-linking of biotinylated-gamma-CAs with streptavidin tetramers. Further addition of an immobilization sequence at amino- or carboxy-terminus also allows for a controlled and reversible immobilization of the gamma-CA to a functionalized surface
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Alber, B.E.; Ferry, J.G.
Characterization of heterologously produced carbonic anhydrase from Methanosarcina thermophila
J. Bacteriol.
178
3270-3274
1996
Methanosarcina thermophila
brenda
Alber, B.E.; Colangelo, C.M.; Dong, J.; Stalhandske, C.M.V.; Baird, T.T.; Tu, C.; Fierke, C.A.; Silverman, D.N.; Scott, R.A.; Ferry, J.G.
Kinetic and spectroscopic characterization of the gamma-carbonic anhydrase from the methanoarcheon Methanosarcina thermophila
Biochemistry
38
13119-13128
1999
Methanosarcina thermophila
brenda
Iverson, T.M.; Alber, B.E.; Kisker, C.; Ferry, J.G.; Rees, D.C.
A closer look at the active site of gamma-class carbonic anhydrases: High resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila
Biochemistry
39
9222-9231
2000
Methanosarcina thermophila (P40881), Methanosarcina thermophila
brenda
Tripp, B.C.; Ferry, J.G.
A structure-function study of a proton transport pathway in teh gamma-class carbonic anhydrase from Methanosarcina thermophila
Biochemistry
39
9232-9240
2000
Methanosarcina thermophila
brenda
Tu, C.; Rowlett, R.S.; Tripp, B.C.; Ferry, J.G.; Silverman, D.N.
Chemical rescue of proton transfer in catalysis by carbonic anhydrases in the beta- and gamma-class
Biochemistry
41
15429-15435
2002
Arabidopsis thaliana, Methanosarcina thermophila
brenda
Tripp, B.C.; Tu, C.; Ferry, J.G.
Role of the arginine 59 in the gamma-class carbonic anhydrases
Biochemistry
41
669-678
2002
Methanosarcina thermophila (P40881)
brenda
Tu, C.; Tripp, B.C.; Ferry, J.G.; Silverman, D.N.
Bicarbonate as a proton donor in catalysis by Zn(II)- and Co(II)-containing carbonic anhydrases
J. Am. Chem. Soc.
123
5861-5866
2001
Homo sapiens, Methanosarcina thermophila
brenda
Alber, B.E.; Ferry, J.G.
A carbonic anhydrase from the archaeon Methanosarcina thermophila
Proc. Natl. Acad. Sci. USA
91
6909-6913
1994
Methanosarcina thermophila (P40881), Methanosarcina thermophila
brenda
Alterio, V.; De Simone, G.; Monti, S.M.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides - solution and crystallographic studies
Bioorg. Med. Chem. Lett.
17
4201-4207
2007
Helicobacter pylori (O24855), Helicobacter pylori (Q1CVF1), Homo sapiens (O43570), Homo sapiens (P00915), Homo sapiens (P00918), Homo sapiens (P07451), Homo sapiens (P22748), Homo sapiens (P23280), Homo sapiens (P35218), Homo sapiens (P43166), Homo sapiens (Q16790), Homo sapiens (Q9ULX7), Homo sapiens (Q9Y2D0), Homo sapiens, Methanosarcina thermophila (P40881), Mus musculus (Q9D6N1)
brenda
Macauley, S.R.; Zimmerman, S.A.; Apolinario, E.E.; Evilia, C.; Hou, Y.M.; Ferry, J.G.; Sowers, K.R.
The archetype gamma-class carbonic anhydrase (Cam) contains iron when synthesized in vivo
Biochemistry
48
817-819
2009
Methanosarcina thermophila
brenda
Innocenti, A.; Zimmerman, S.A.; Scozzafava, A.; Ferry, J.G.; Supuran, C.T.
Carbonic anhydrase activators: activation of the archaeal beta-class (Cab) and gamma-class (Cam) carbonic anhydrases with amino acids and amines
Bioorg. Med. Chem. Lett.
18
6194-6198
2008
Methanothermobacter thermautotrophicus, Methanosarcina thermophila
brenda
Amata, O.; Marino, T.; Russo, N.; Toscano, M.
Catalytic activity of a zeta-class zinc and cadmium containing carbonic anhydrase. Compared work mechanisms
Phys. Chem. Chem. Phys.
13
3468-3477
2011
Methanosarcina thermophila, Conticribra weissflogii
brenda
Zimmerman, S.; Domsic, J.F.; Tu, C.; Robbins, A.H.; McKenna, R.; Silverman, D.N.; Ferry, J.G.
Role of Trp19 and Tyr200 in catalysis by the gamma-class carbonic anhydrase from Methanosarcina thermophila
Arch. Biochem. Biophys.
529
11-17
2013
Methanosarcina thermophila (P40881), Methanosarcina thermophila
brenda
Innocenti, A.; Zimmerman. S.; Ferry, J.G.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors. Inhibition of the zinc and cobalt gamma-class enzyme from the archaeon Methanosarcina thermophila with anions
Bioorg. Med. Chem. Lett.
14
3327-3331
2004
Methanosarcina thermophila, Methanosarcina thermophila (P40881)
brenda
Zimmerman, S.; Innocenti, A.; Casini, A.; Ferry, J.G.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors. Inhibition of the prokariotic beta and gamma-class enzymes from Archaea with sulfonamides
Bioorg. Med. Chem. Lett.
14
6001-6006
2004
Methanothermobacter thermautotrophicus, Methanosarcina thermophila (P40881), Methanosarcina thermophila
brenda
Kisker, C.; Schindelin, H.; Alber, B.E.; Ferry, J.G.; Rees, D.C.
A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila
EMBO J.
15
2323-2330
1996
Methanosarcina thermophila (P40881), Methanosarcina thermophila
brenda
Zimmerman, S.A.; Tomb, J.F.; Ferry, J.G.
Characterization of CamH from Methanosarcina thermophila, founding member of a subclass of the gamma class of carbonic anhydrases
J. Bacteriol.
192
1353-1360
2010
Methanosarcina thermophila (C3W4Q7), Methanosarcina thermophila TM-1 (C3W4Q7)
brenda
Tripp, B.C.; Bell, C.B.; Cruz, F.; Krebs, C.; Ferry, J.G.
A role for iron in an ancient carbonic anhydrase
J. Biol. Chem.
279
6683-6687
2004
Methanosarcina thermophila, Methanosarcina thermophila (P40881)
brenda
Simler, B.R.; Doyle, B.L.; Matthews, C.R.
Zinc binding drives the folding and association of the homo-trimeric gamma-carbonic anhydrase from Methanosarcina thermophila
Protein Eng. Des. Sel.
17
285-291
2004
Methanosarcina thermophila
brenda
Di Fiore, A.; Alterio, V.; Monti, S.M.; De Simone, G.; D'Ambrosio, K.
Thermostable carbonic anhydrases in biotechnological applications
Int. J. Mol. Sci.
16
15456-15480
2015
Methanosarcina thermophila, Sulfurihydrogenibium azorense, Citrobacter freundii (A0A0D7LLM5), Caminibacter mediatlanticus (A6DAW8), Sulfurihydrogenibium sp. YO3AOP1 (B2V8E3), Persephonella marina (C0QRB5), Methanothermobacter thermautotrophicus (D9PU79), Thermovibrio ammonificans (E8T502), Serratia sp. ISTD04 (K4N028), Pyrococcus horikoshii (O59257), Homo sapiens (P00918), Bos taurus (P00921), Desulfovibrio vulgaris (Q72B61), Caminibacter mediatlanticus TB-2 (A6DAW8), Desulfovibrio vulgaris Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303 (Q72B61), Persephonella marina DSM 14350 / EX-H1 (C0QRB5), Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg (D9PU79), Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1 (E8T502)
brenda