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Enzyme Nomenclature
Information on EC 1.2.7.4 - anaerobic carbon-monoxide dehydrogenase
for references in articles please use BRENDA:EC1.2.7.4
Word Map on EC 1.2.7.4
- 1.2.7.4
-
methanosarcina
-
codhs
- thermophila
- hydrogenoformans
-
carboxydothermus
-
nifec
-
wood-ljungdahl
- thermoaceticum
-
acetogenic
-
acetate-grown
- moorella
-
square-planar
-
a-cluster
-
co-oxidizing
- analysis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.2.7.4
-
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RECOMMENDED NAME
GeneOntology No.
anaerobic carbon-monoxide dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
CO may react with OH- rather than with H2O
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
ping-pong mechanism
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
ping-pong mechanism
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
enzyme also catalyzes acetyl-CoA/CoA and acetyl-CoA/CO exchange reaction, enzyme has both CO-dehydrogenase and acetyl-CoA synthase activity
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
kinetics, oxidation state of Fe-S cluster during catalysis
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
mechanism, CO binding labilizes the hydroxyl bridging Ni and Fe and increases the nucleophilic tendency toward attacking Ni-bound carbonyl
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
mechanism, CO binding labilizes the hydroxyl bridging Ni and Fe and increases the nucleophilic tendency toward attacking Ni-bound carbonyl
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
mechanism, enzyme is capable of producing formate
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
CO2/CO tunnel gating mechanism
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
mechnaism via thiocarbonate-like intermediate state
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
CO and CO2 enter and exit the enzyme at the water channel along the betabeta subunit interface. CO either enters the enzyme and migrates through the tunnel before binding at the A-cluster, or it binds the A-cluster directly from solvent
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
anaerobic CO dehydrogenases catalyze the reversible oxidation of CO to CO2 at a complex Ni-, Fe-, and S-containing metal center called cluster C
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
carbon-monoxide,water:ferredoxin oxidoreductase
This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [4Fe-4S] D-cluster; and two [4Fe-4S] B-clusters. In methanogenic archaea additional [4Fe-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY
64972-88-9
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
more than threefold induction of enzyme activity and increase in enzyme expression in a mutant lacking the membrane-bound energy-conserving hydrogenase Ehb
-
-
grows on acetate if cocultured with hydrogen-consuming methanogenic partner Methanothermobacter thermautrophicus
-
-
enzyme CooS in complex with an electron transfer protein CooF and a membrane bound [Ni-Fe] hydrogenase
-
-
-
390451, 390453, 390457, 390458, 390460, 390461, 390462, 390467, 390468, 390469, 390475, 390476, 390480, 390481, 654754, 655797, 674925, 684432, 685091, 687824
-
-
bifunctional acetyl-coenzyme A synthase/carbon monoxide dehydrogenase, isolated alpha subunit
-
-
bifunctional enzyme with carbon-monoxide dehydrogenase/acetyl coenzyme A synthase activity
-
-
CODH/ACS subunit beta; formerly Clostridium thermoaceticum strain ATCC 39073
UniProt
large, medium and small subunit
D5G1Y2, D5G1Y0, D5G1Y1
UniProt
P19919 large subunit, P19920 medium subunit, P19921 small subunit
UniProt
purple nonsulfur bacterium, the enzyme exists in the forms, I and II, which differ in metal content
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
-
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-SCoA + CO
acetyl-SCoA + CO
-
acetyl-CoA/CO exchange reaction, 14C experiments prove that the enzyme can cleave both the carbon-carbon and carbon-sulfur bonds of acetyl-CoA as well as to store methyl, CO, and CoA fragments at the active site
-
r
acetyl-SCoA + CoASH
acetyl-SCoA + CoASH
-
acetyl-CoA/CoA exchange reaction
-
r
CO + ferredoxin
?
-
ferredoxin is the direct electron acceptor, the carbon-monoxide dehydrogenase complex reduces a ferredoxin which, together with membranes and associated hydrogenase, reconstitutes a CO-oxidizing:H2-evolving system
-
-
?
CO + H2O + 1,1'-trimethylene-4,4'-dimethyl-2,2'dipyridylium dibromide
CO2 + reduced 1,1'-trimethylene-4,4'-dimethyl-2,2'dipyridylium dibromide
-
-
-
?
CO + H2O + 2,3,5-triphenyltetrazolium chloride
CO2 + reduced 2,3,5-triphenyltetrazolium chloride
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO + H2O + cytochrome c3
CO2 + reduced cytochrome c3
-
cytochrome 3 from Desulfovibrio vulgaris
-
?
CO + H2O + electron acceptor
CO2 + reduced electron acceptor
-
a proton gradient across the cytoplasmic membrane is generated by channeling the electrons formed via cytochrome b561 into a CO-insensitive respiratory chain
-
?
CO + H2O + methylene blue
CO2 + reduced methylene blue + H2
-
-
-
-
?
CO + H2O + oxidized 2,3,5-triphenyltetrazolium chloride
CO2 + reduced 2,3,5-triphenyltetrazolium chloride
-
-
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO + H2O + oxidized cytochrome b
CO2 + reduced cytochrome b
-
membrane-bound b-type, native electron carrier
-
-
?
CO + H2O + oxidized cytochrome c3
CO2 + reduced cytochrome c3
-
Desulfovibrio vulgaris cytochrome c3
-
-
?
CO + H2O + oxidized methylene blue
CO2 + reduced methylene blue
-
-
-
-
?
CO + H2O + oxidized phenazine methosulfate
CO2 + reduced phenazine methosulfate
-
-
-
-
?
CO + H2O + oxidized rubredoxin
CO2 + reduced rubredoxin
-
most efficient electron acceptor
-
-
?
CO + H2O + phenazine methosulfate
CO2 + reduced phenazine methosulfate
-
-
-
?
propionyl-SCoA + CoASH
propionyl-SCoA + CoASH
-
acetyl-CoA/CoA exchange reaction
-
r
trichloroethylene + ?
cis-dichloroethylene + trans-dichlororethylene + 1,1-dichloroethylene + vinyl chloride + ethylene
-
-
-
?
CO + H2O + 2,3,5-triphenyltetrazolium chloride
CO2 + reduced 2,3,5-triphenyltetrazolium chloride
-
-
-
?
CO + H2O + 2,3,5-triphenyltetrazolium chloride
CO2 + reduced 2,3,5-triphenyltetrazolium chloride
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
Mycobacterium sp. DSM 3803 / JC1
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
Mycobacterium tuberculosis H37Ra / ATCC 25177
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
Mycobacterium tuberculosis TMC 326 / H37Ra-INH-R / ATCC 35835
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
r
CO + H2O + acceptor
CO2 + reduced acceptor
D5G1Y2; D5G1Y0; D5G1Y1;
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + coenzyme F420
CO2 + reduced coenzyme F420
-
1.5% of the activity with methyl viologen
-
?
CO + H2O + coenzyme F420
CO2 + reduced coenzyme F420
-
-
-
?
CO + H2O + electron acceptor
?
-
the physiological role of the enzyme in acetyl-CoA synthesis is the reduction of CO2 to a bound CO, the physiological electron acceptor is not known and may be different in different organisms
-
-
?
CO + H2O + electron acceptor
?
-
key enzyme in C1-pathway of acetyl-CoA degradation
-
-
?
CO + H2O + electron acceptor
?
Autotrophic methanogenic bacterium
-
the enzyme is required for autotrophic CO2 fixation in methanogens, the enzyme is also involved in methanogenesis from acetate, not required for methanogenesis
-
-
?
CO + H2O + electron acceptor
?
-
the carbon monoxide dehydrogenase-corrinoid enzyme complex catalyzes the methylation of tetrahydrosarcinapterin in a reaction involving net cleavage of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
enzyme may also be involved in the formation of acetyl-CoA from methanol in methanogens
-
-
?
CO + H2O + electron acceptor
?
-
extensive role of the enzyme in the acetyl-CoA pathway, it is proposed that the enzyme serves as the CO, CH3, SCoA acceptor and catalyzes the final steps of the synthesis of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
the enzyme is involved in the Wood pathway of acetyl-CoA synthesis
-
-
?
CO + H2O + electron acceptor
?
-
delivery of a low-potential electron to the CO-bound NiFe complex is the physiological function of the CO oxidation reaction catalyzed by the enzyme
-
-
?
CO + H2O + electron acceptor
?
-
the formation of acetyl-CoA from methyltetrahydrofolate requires several enzymes, including CO dehydrogenase
-
-
?
CO + H2O + electron acceptor
?
-
ferredoxin and a membrane-bound b-type cytochrome are considered to be the native electron carriers
-
-
?
CO + H2O + electron acceptor
?
-
catalyzes the final step in the synthesis of acetyl-CoA
-
-
-
CO + H2O + electron acceptor
?
-
catalyzes the final step in the synthesis of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
the physiological role of the enzyme in acetyl-CoA synthesis is the reduction of CO2 to a bound CO, the physiological electron acceptor is not known and may be different in different organisms
-
-
?
CO + H2O + electron acceptor
?
-
key role of the enzyme in the synthesis of acetyl-CoA
-
-
?
CO + H2O + FAD
CO2 + FADH2
-
0.3% of the activity with methyl viologen
-
?
CO + H2O + FAD
CO2 + FADH2
-
at 15% of the specific activity compared to methyl viologen
-
-
?
CO + H2O + FAD
CO2 + FADH2
-
at 15% of the specific activity compared to methyl viologen
-
-
?
CO + H2O + ferredoxin
CO2 + reduced ferredoxin
-
active with ferredoxin obtained from Clostridium thermoaceticum, no activity with ferredoxin from spinach
-
?
CO + H2O + FMN
CO2 + FMNH2
-
0.6% of the activity with methyl viologen
-
?
CO + H2O + FMN
CO2 + FMNH2
-
at 15% of the specific activity compared to methyl viologen
-
-
?
CO + H2O + FMN
CO2 + FMNH2
-
at 15% of the specific activity compared to methyl viologen
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
r
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
r
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
optimal concentration of CO 5% in headspace
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
Carboxydothermus hydrogenoformans Z-2901 / DSM 6008
-
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
no activity with NAD+ and NADP+
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
the enzyme fails to reduce NAD+, NADP+, or 8-hydroxy-5-deazaflavin cofactor 420
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
r
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes the exchange reaction between coenzyme A and acetyl-CoA
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes the exchange reaction between coenzyme A and acetyl-CoA
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes the exchange reaction between propionyl-CoA and CoA at 7% of the exchange with acetyl-CoA
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes at a low rate an exchange between CO2 and the carbonyl group of acetyl-CoA
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
no activity with FAD, NAD+ and NADP+
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes the synthesis of acetyl-CoA from methyl corrinoid, Co and CoASH
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes reversible decarbonylation of acetyl-CoA with retention of stereochemistry at the methyl group
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
?
CO + H2O + methylene blue
CO2 + reduced methylene blue
-
-
-
?
CO + H2O + NAD+
CO2 + NADH + H+
-
the specific activity is increased by approximately 20% with NAD+ as the electron acceptor compared to methyl viologen
-
-
?
CO + H2O + NAD+
CO2 + NADH + H+
-
the specific activity is increased by approximately 20% with NAD+ as the electron acceptor compared to methyl viologen
-
-
?
CO + H2O + NADP+
CO2 + NADPH + H+
-
the specific activity is increased by approximately 20% with NADP+ as the electron acceptor compared to methyl viologen
-
-
?
CO + H2O + NADP+
CO2 + NADPH + H+
-
the specific activity is increased by approximately 20% with NADP+ as the electron acceptor compared to methyl viologen
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
D5G1Y2; D5G1Y0; D5G1Y1;
-
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
D5G1Y2; D5G1Y0; D5G1Y1;
-
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
may participate in methanogenesis by cleavage of acetate, reverse of the reaction in acetate biosynthesis
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
-
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
ferredoxin I and II
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
ferredoxin from Clostridium pasteurianum is also a substrate
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
acetate biosynthesis pathway, catalyzes an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
initial step of CO metabolism in acetogenic bacteria
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
-
-
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
-
-
-
-
?
CO + H2O + oxidized flavodoxin
CO2 + reduced flavodoxin
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
no enzyme with cofactor F420
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
no enzyme with cofactor F420
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen + H+
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen + H+
-
-
-
-
?
CO + H2O + rubredoxin
CO2 + reduced rubredoxin
-
most efficient electron acceptor
-
?
CO + H2O + rubredoxin
CO2 + reduced rubredoxin
-
most efficient electron acceptor
-
?
tetrahydrosarcinapterin + acetyl-SCoA + H2O
methyltetrahydrosarcinapterin + CO2 + CoASH
-
-
-
-
tetrahydrosarcinapterin + acetyl-SCoA + H2O
methyltetrahydrosarcinapterin + CO2 + CoASH
-
carbon monoxide dehydrogenase-corrinoid enzyme complex, enzyme complex functions in synthesis of acetyl-CoA
-
r
additional information
?
-
-
enzyme fails to reduce NAD+, NADP+ or the 8-hydroxy-5-deazaflavin factor F420
-
-
-
additional information
?
-
-
pure enzyme has no hydrogenase or formate dehydrogenase activity
-
-
-
additional information
?
-
-
spinach ferredoxin, FAD, NAD+ and NADP+ are not reduced
-
-
-
additional information
?
-
-
Thermacetogenium phaeum operates the CO dehydrogenase/acetyl-CoA pathway reversibly both in acetate oxidation and in reductive acetogenesis by using the same biochemical apparatus
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CO + ferredoxin
?
-
ferredoxin is the direct electron acceptor, the carbon-monoxide dehydrogenase complex reduces a ferredoxin which, together with membranes and associated hydrogenase, reconstitutes a CO-oxidizing:H2-evolving system
-
-
?
CO + H2O + electron acceptor
CO2 + reduced electron acceptor
-
a proton gradient across the cytoplasmic membrane is generated by channeling the electrons formed via cytochrome b561 into a CO-insensitive respiratory chain
-
?
CO + H2O + oxidized cytochrome b
CO2 + reduced cytochrome b
-
membrane-bound b-type, native electron carrier
-
-
?
additional information
?
-
-
Thermacetogenium phaeum operates the CO dehydrogenase/acetyl-CoA pathway reversibly both in acetate oxidation and in reductive acetogenesis by using the same biochemical apparatus
-
-
-
CO + H2O + acceptor
CO2 + reduced acceptor
Q9F8A8
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
D5G1Y2 and D5G1Y0 and D5G1Y1
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
D5G1Y2 and D5G1Y0 and D5G1Y1
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
P19919 and P19920 and P19921
-
-
-
?
CO + H2O + electron acceptor
?
-
the physiological role of the enzyme in acetyl-CoA synthesis is the reduction of CO2 to a bound CO, the physiological electron acceptor is not known and may be different in different organisms
-
-
?
CO + H2O + electron acceptor
?
-
key enzyme in C1-pathway of acetyl-CoA degradation
-
-
?
CO + H2O + electron acceptor
?
Autotrophic methanogenic bacterium
-
the enzyme is required for autotrophic CO2 fixation in methanogens, the enzyme is also involved in methanogenesis from acetate, not required for methanogenesis
-
-
?
CO + H2O + electron acceptor
?
-
the carbon monoxide dehydrogenase-corrinoid enzyme complex catalyzes the methylation of tetrahydrosarcinapterin in a reaction involving net cleavage of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
enzyme may also be involved in the formation of acetyl-CoA from methanol in methanogens
-
-
?
CO + H2O + electron acceptor
?
-
extensive role of the enzyme in the acetyl-CoA pathway, it is proposed that the enzyme serves as the CO, CH3, SCoA acceptor and catalyzes the final steps of the synthesis of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
the enzyme is involved in the Wood pathway of acetyl-CoA synthesis
-
-
?
CO + H2O + electron acceptor
?
-
delivery of a low-potential electron to the CO-bound NiFe complex is the physiological function of the CO oxidation reaction catalyzed by the enzyme
-
-
?
CO + H2O + electron acceptor
?
-
the formation of acetyl-CoA from methyltetrahydrofolate requires several enzymes, including CO dehydrogenase
-
-
?
CO + H2O + electron acceptor
?
-
ferredoxin and a membrane-bound b-type cytochrome are considered to be the native electron carriers
-
-
?
CO + H2O + electron acceptor
?
-
catalyzes the final step in the synthesis of acetyl-CoA
-
-
-
CO + H2O + electron acceptor
?
-
catalyzes the final step in the synthesis of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
the physiological role of the enzyme in acetyl-CoA synthesis is the reduction of CO2 to a bound CO, the physiological electron acceptor is not known and may be different in different organisms
-
-
?
CO + H2O + electron acceptor
?
-
key role of the enzyme in the synthesis of acetyl-CoA
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
may participate in methanogenesis by cleavage of acetate, reverse of the reaction in acetate biosynthesis
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
acetate biosynthesis pathway, catalyzes an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
initial step of CO metabolism in acetogenic bacteria
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
-
-
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ni-Fe-S center
-
uses a Ni-Fe-S center called the C-cluster to reduce carbon dioxide to carbon monoxide and uses a second Ni-Fe-S center, called the A-cluster, to assemble acetyl-CoA from a methyl group, coenzyme A, and C-cluster-generated CO
-
flavin adenine dinucleotide
-
suggested from gene sequence analysis
flavin adenine dinucleotide
-
cofactor is released upon treatment with guanidine-HCl, SDS, heat or acid
molybdopterin cytosine dinucleotide
-
suggested from gene sequence analysis
molybdopterin cytosine dinucleotide
-
cofactor is buried at the center of the L subunit
molybdopterin cytosine dinucleotide
-
cofactor is released upon treatment with guanidine-HCl, SDS, heat or acid
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S cluster
-
core extrusion experiments indicate 6 [4Fe-4S] clusters per tetramer, and electron paramagnetic resonance spectroscopy detects at least one of these clusters, in the reduced form
copper
Cu2+
Fe-S center
-
the multifunctional enzyme complex contains iron-sulfur centers
Fe2+
Iron
Molybdenum
Ni2+
Nickel
Zinc
[2Fe-2S]-center
-
the small subunit contains two [2Fe-2S] centers
additional information
copper
-
dinuclear heterometal [CuSMo(=O)OH] cluster in the active site
copper
-
synthesis and characterization of dinuclear Mo-Cu complexes relevant to the active site of MoCu-enzyme by X-ray diffraction studies and by reactivity
Fe2+
-
contains a [NiFe4S5] center called cluster C; Ni-, Fe-, and S-containing metal center called cluster C
Fe2+
-
CODHII contains iron, the active site of CODH contains a [NiFe4S4OHx] cluster known as C-cluster
Iron
-
the alphabeta dimer contains approximately 9-11 mol of iron and 12-14 mol of acid-labile sulfur per mol of dimer
Iron
-
0.58, 0.67 and 1.96 atoms of iron per mol of large, medium- and small subunit, two iron-sulfur centers are associated with the small subunit
Iron
-
contains 25 mol of Fe2+ and 20 mol of S2- per mol of tetramer, the enzyme contains 2 (4Fe-4S)+ clusters
Iron
-
CO dehydrogenase complex consists of a two-subunit nickel/iron-sulfur component and the two-subunit factor III-containing corrinoid/iron-sulfur (Co/Fe-S) component
Iron
-
enzyme contains 3 iron containing centers: center A contains nickel and iron and is suggested to be the acetyl-CoA cleavage site, center B is a [4Fe-4S]2+/1+ center, center C is a fast relaxing center
Iron
-
CO oxidation occurs at Ni- and FeS containing center C, electrons are transferred from cluster C via center B to external electron acceptors; the alphabeta dimer contains approximately 9-11 mol of iron and 12-14 mol of acid-labile sulfur per mol of dimer
Iron
-
contains 11 mol of iron and 14 mol of acid-labile sulfur per mol of alphabeta dimer
Iron
-
the NiFe complex is required for catalyzing the exchange reaction and the acetyl-CoA synthase reaction
Iron
-
enzyme form I contains 7 iron and 6 sulfur per monomer; enzyme form II contains 9 iron and 8 sulfur per monomer
Iron
-
the enzyme contains two metal centers: a Ni-X-[4Fe-4S]2+/1+ cluster, i.e. C-center, that serves as the CO-oxidation site and a standard [Fe4S4]2+/1+ cluster, i.e. B-center, that mediates electron flow from the C-center to the external electron acceptor
Iron
-
enzyme utilizes three types of Fe-S clusters: a [Ni4Fe5S] C-cluster catalyzing the CO oxidation, and 2 distinct [4Fe4S] electron-transfer sites called clusters B and D
Molybdenum
-
molybdopterin-cytosine dinucleotide cofactor is composed of a molybdenum ion with 2 oxo- and 1 hydroxoligand complexed by the enedithiolene group of molybdopterin
Molybdenum
-
dinuclear heterometal [CuSMo(=O)OH] cluster in the active site
Molybdenum
-
synthesis and characterization of dinuclear Mo-Cu complexes relevant to the active site of MoCu-enzyme by X-ray diffraction studies and by reactivity
Ni2+
-
contains a [NiFe4S5] center called cluster C; Ni-, Fe-, and S-containing metal center called cluster C
Ni2+
-
CODHII contains nickel, the active site of CODH contains a [NiFe4S4OHx] cluster known as C-cluster
Ni2+
-
Ni is tightly bound to the enzyme and is not removed by anaerobic dialysis or gel permeation
Ni2+
-
contains Ni2+-activated alpha subunits, Ni2+ is required for activity and oligomerization
Nickel
-
the alphabeta dimer contains approximately 2 mol of nickel per mol of dimer
Nickel
-
carbon monoxide dehydrogenase II, enzyme contains 5 metal clusters, a [Ni-4Fe-5S] cluster appears to be the active site of CO oxidation
Nickel
-
CO dehydrogenase complex consists of a two-subunit nickel/iron-sulfur component and the two-subunit factor III-containing corrinoid/iron-sulfur (Co/Fe-S) component
Nickel
-
the alphabeta dimer contains approximately 2 mol of nickel per mol of dimer
Nickel
-
both CO and CoASH bind near the nickel site, nickel may therefore be the active metal center for C-C bond formation
Nickel
-
the NiFe complex is required for catalyzing the exchange reaction and the acetyl-CoA synthase reaction
Nickel
-
enzyme form I contains 0.6 mol of nickel per mol of monomer; enzyme form II contains 1.4 mol of nickel per mol of monomer
Nickel
-
the enzyme contains two metal centers: a Ni-X-[4Fe-4S]2+/1+ cluster, i.e. C-center, that serves as the CO-oxidation site and a standard [4Fe-4S]2+/1+ cluster, i.e. B-center, that mediates electron flow from the C-center to the external electron acceptor, the nickel cation is proposed to be Ni2+ of the oxidized state of the C-center and in the one-electron-reduced state of the C-center, appears to strongly affect the redox behavior of the [4Fe-4S]2+/1+ component of the C-center
Nickel
-
wild-type, 0.85 mol per mol of enzyme. Analysis of activation of wild-type and mutant apo-enzymes by nickel
Nickel
-
synthesis of an analogue of the C-cluster of Carboxydothermus hydrogenoformans with a planar Ni(II) site and attachment of an exo iron atom in the core unit NiFe4S5 and analysis of products
Zinc
-
the alphabeta dimer contains approximately 1 mol of zinc per mol of dimer
Zinc
-
the alphabeta dimer contains approximately 1 mol of zinc per mol of dimer
Zinc
-
enzyme form I contains 0.4 mol of zinc per mol of monomer; enzyme form II contains 0.8 mol of zinc per mol of monomer
additional information
-
no stimulation by MgSO4, CoCl2, NiCl2 and ZnSO4
additional information
-
the enzyme contains 30 Fe, 2 Ni, 1 Zn, and 1 Cu (per alpha 2 beta 2 enzyme)
additional information
-
no oligomerization or activity in the presence of Co2+, Zn2+, and Cu2+, oligomerization but no exhibition of catalytic activity in the presence of Pd2+ and Pt2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
1 mM, inactivates CO/acetyl-CoA exchange activity completely but has no effect on CO oxidation
COS
-
rapid-equilibrium inhibitor largely competitive versus CO, uncompetitive versus methyl viologen
D-glucose
partially inhibited by incubation with 0.5 mM exogenous D-glucose
Glyoxaldehyde
-
inactivation requires enzymatic turnover; only with CO and methyl viologen as substrates
potassium cyanide
-
competitive inhibitor of reduced CODHII with respect to the substrate CO, inhibition of dithionite- or Ti(III) citrate-reduced CODHII by potassium cyanide is fully reversible since the enzyme can be completely reactivated, sodium sulfide has no effect on the reactivation of cyanide-inhibited CODHII in the presence of dithionite
CN-
-
0.2 mM, 17% inhibition in the presence of air, 32% CO and 69% N2, inhibition can be removed by O2 or CO
CN-
-
CO, CO2 and COS reverse inhibition; dithionite slows the inhibition, but cannot reactivate the enzyme
CN-
-
CO and COS protect from inhibition; CO, CO2 and COS reverse inhibition
cyanide
-
0.075 mM, reversible, competitive inhibition of reduced CODHII with respect to the substrate carbon monoxide, which protects reduced CODHII against inhibition by cyanide, inhibited CODHII regains initial activity after a 15-25-min incubation at 70°C with dithionite or Ti(III) citrate under CO or N2, while slower and partial reactivation to 30-50% of the initial activity occurs with dithiothreitol or without reductants
KCN
-
CO reverses cyanide inhibition, but promotes reaction with methyl iodide
additional information
-
dimethylglyoxime is no inhibitor, formaldehyde and acetaldehyde does not inactivate the enzyme; not inhibited by 20 mM formaldehyde or acetaldehyde
-
additional information
-
not affected by propyl iodide, methyl iodide, carbon tetrachloride,or metal chelators; not inhibited by propyl iodide, methyl iodide, carbon tetrachloride, EDTA or nitrilotriacetate
-
additional information
-
phenylglyoxal, methylglyoxal, butanedione, mersalyl acid, methyl iodide, 5,5'-dithiobis (2-nitrobenzoate) and sodium dithionite inhibits the exchange reaction between CO and acetyl-CoA
-
additional information
-
inhibition data are interpreted in terms of two binding sites for CO on CO dehydrogenase
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
corrinoid cofactor
-
the multifunctional enzyme complex contains a corrinoid cofactor
-
Nickel
-
Ni-activated alpha subunit rapidly and reversibly accepts a methyl group
Ti(III)citrate
-
1mM for 1 min at 65°C, 45fold increase in initial activity
additional information
-
CooC proteins are ATPases involved in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenases
-
sodium nitroprusside
-
5 mM sodium nitroprusside induces CO-DH gene expression after 20 min exposure; activity increases in the presence of 5 mM sodium nitroprusside during 20 min incubation
sodium nitroprusside
-
5 mM sodium nitroprusside induces CO-DH gene expression after 20 min exposure; activity increases in the presence of 5 mM sodium nitroprusside during 20 min incubation
sodium nitroprusside
-
5 mM sodium nitroprusside induces CO-DH gene expression after 20 min exposure; activity increases in the presence of 5 mM sodium nitroprusside during 20 min incubation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00295
methylene blue
-
Ag+-substituted enzyme, at pH 7.0 and 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
42000/min/Ni, substrate methyl viologen
-
additional information
additional information
-
pH 5.3, 50°C, activity of CO oxidation to CO2, ferredoxin II as electron carrier, turnover number is approximately 780 mol/mol of CO dehydrogenase
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0217
cyanide
-
at 23°C, in 4 mM dithionite, and 4 mM dithiothreitol
1.2
pivaloylpantetheine-SH
-
inhbition of CO/acetyl-CoA exchange reaction
0.4
CO
-
noncompetitive inhibition of the acetyl-CoA exchange reaction
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.4
0.96
-
after 12.92fold purification, at 95°C, pH 8.0, using methylene blue as electron acceptor
2.08
-
after 12.92fold purification, at 95°C, pH 8.0, using methyl viologen as electron acceptor
2.45
-
after 12.92fold purification, at 95°C, pH 8.0, using NADP+ as electron acceptor
2.47
-
after 12.92fold purification, at 95°C, pH 8.0, using NAD+ as electron acceptor
5.7
-
CO oxidation in cell-extracts at 85°C, electron acceptor methylviologen
7
-
acetyl-CoA/CoA exchange reaction at pH 6.0 and 45°C, 100% CO in the gas phase
28
-
acetyl-CoA/CoA exchange reaction at pH 6.0 and 45°C, CO in the gas phase replaced by N2
additional information
0.4
-
enzyme activity in cell extracts at 35°C, pH 7.5, 100% CO in gas phase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
7.5
8.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
pH 6.5: about 25% of maximal activity, pH 8-9: maximal activity
8 - 11.5
-
pH 8: about 55% of maximal activity, pH 11.5: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75 - 100
-
about 65% activity at 75°C, about 75% activity at 80°C, about 80% activity at 85°C, about 90% activity at 90°C, 100% activity at 95°C, about 30% activity at 100°C, respectively
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity of one of the CO dehydrogenases is sixfold greater in acetate-grown compared with methanol-grown cells
-
activity of one of the CO dehydrogenases is sixfold greater in acetate-grown compared with methanol-grown cells
-
-
induced with 100% CO 24 h before harvesting
-
activity of one of the CO dehydrogenases is sixfold greater in acetate-grown compared with methanol-grown cells
-
activity of one of the CO dehydrogenases is sixfold greater in acetate-grown compared with methanol-grown cells
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303);
Q46G04
Methanosarcina barkeri (strain Fusaro / DSM 804);
Moorella thermoacetica;
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q9F8A8
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q3AE44
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901);
Q72A99
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303);
Q72A99
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303);
Q72A99
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303);
Q72A99
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303);
Q72A99
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17390
D5G1Y2; D5G1Y0; D5G1Y1;
small subunit, calculated from sequence of cDNA
17752
-
L2,M2,S2, 2 * 87224 + 2 * 30694 + 2 * 17752, deduced from gene sequence, SDS-PAGE
17800
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
19000
19700
30200
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
30620
D5G1Y2; D5G1Y0; D5G1Y1;
medium subunit, calculated from sequence of cDNA
30694
-
L2,M2,S2, 2 * 87224 + 2 * 30694 + 2 * 17752, deduced from gene sequence, SDS-PAGE
50000
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
51400
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
53000
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
58000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
60000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
62000
-
2 * 62000, enzyme, + electron transfer protein CooF and membrane bound [Ni-Fe] hydrogenase, six differentsubunits; 2 * 62000, SDS-PAGE, enzyme
63200
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
70000
71000
73000
-
alpha2,beta2, 2 * 82000 + 2 * 73000, enzyme previously thought to have an alpha3,beta3 structure, SDS-PAGE
78000
82000
-
alpha2,beta2, 2 * 82000 + 2 * 73000, enzyme previously thought to have an alpha3,beta3 structure, SDS-PAGE
84500
85970
D5G1Y2; D5G1Y0; D5G1Y1;
large subunit, calculated from sequence of cDNA
87224
-
L2,M2,S2, 2 * 87224 + 2 * 30694 + 2 * 17752, deduced from gene sequence, SDS-PAGE
88700
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
89000
161000
250000
1000000
-
the native enzyme (MW 250000 Da) forms aggregates with an MW of approximately 1000000, gradient gel electrophoresis
1600000
-
carbon monoxide dehydrogenase-corrinoid enzyme complex, gel filtration
3000000
-
high molecular weight form exists under conditions of high ionic strength, gel filtration
additional information
19000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
19700
-
2 * 19700 + 2 * 84500, alpha2beta2, SDS-PAGE; 2 * 84500 + 2 * 19700, alpha2beta2, SDS-PAGE
19700
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
71000
-
3 * 71000, beta, + 3 * 78000, alpha, SDS-PAGE; 3 * 78000 + 3 * 71000, alpha3,beta3, SDS-PAGE
71000
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
71000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
78000
-
3 * 71000, beta, + 3 * 78000, alpha, SDS-PAGE; 3 * 78000 + 3 * 71000, alpha3,beta3, SDS-PAGE
78000
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
84500
-
2 * 19700 + 2 * 84500, alpha2beta2, SDS-PAGE; 2 * 84500 + 2 * 19700, alpha2beta2, SDS-PAGE
84500
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
89000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
250000
-
the native enzyme (MW 250000 Da) forms aggregates with an MW of approximately 1000000, gradient gel electrophoresis
additional information
-
the enzyme is part of a high molecular mass multienzyme complex that contains a corrinoid protein and carbon monoxide dehydrogenase and requires tetrahydrosarcinapterin as methyl group acceptor
additional information
-
CO dehydrogenase complex consists of a two-subunit nickel/iron-sulfur component and the two-subunit factor III-containing corrinoid/iron-sulfur (Co/Fe-S) component
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
hexamer
homodimer
octamer
-
2 * 62000, enzyme, + electron transfer protein CooF and membrane bound [Ni-Fe] hydrogenase, six differentsubunits
oligomer
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
tetramer
additional information
-
properties of enzyme in complex with protein CooF which mediates electron transfer from enzyme to the CO-induced hydrogenase
?
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
?
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
-
hexamer
-
L2,M2,S2, 2 * 87224 + 2 * 30694 + 2 * 17752, deduced from gene sequence, SDS-PAGE
hexamer
-
3 * 71000, beta, + 3 * 78000, alpha, SDS-PAGE; 3 * 78000 + 3 * 71000, alpha3,beta3, SDS-PAGE
hexamer
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
hexamer
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
tetramer
-
alpha2,beta2, 2 * 82000 + 2 * 73000, enzyme previously thought to have an alpha3,beta3 structure, SDS-PAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
carbon monoxide dehydrogenase II, hanging drop vapor diffusion, 20% 2-propanol, 20% polyethylene glycol 3000, 100 mM HEPES, pH 7.5
-
in presence of dithiothreitol or dithionite and under an atmosphere of N2 or CO
-
vapor diffusion, 800 mM KH2PO4, 800 mM NaH2PO4, 2% 2-methyl-2,4-pentanediol, 100 mM HEPES, pH 7.3
-
EPR studies of enzyme in complex with protein CooF which mediates electron transfer from enzyme to the CO-induced hydrogenase, in presence and absence of nickel
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
wild-type and mutants apo-enzymes, stable for at least 30 min within this range
674921
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
-
10 min, about 30% loss of activity in presence of CO, stable in absence of CO
25 - 70
-
purification can be done at 25°C without loss of activity, heating for 30 min at 67°C leads to apparent loss, heating for only a few min at 70°C activates the enzyme
39
-
10 min, 45% loss of activity in presence of CO, stable in absence of CO
62
-
10 min, about 65% loss of activity in presence of CO, about 5% loss of activity in absence of CO
80
-
10 min, about 85% loss of activity in presence of CO, about 20% loss of activity in absence of CO
80 - 104
-
most of the activity remains after heating at 80°C, nearly complete inactivation after heating at 104°C, greater loss of activity at all temperatures when heated in presence of CO
104
-
10 min, complete loss of activity in presence or in absence of CO
additional information
-
CO renders the enzyme more susceptible to temperature inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
100% of activity remains after 48 h of oxygen exposure, and after 168 h of air exposure, activity is 88% of the initial activity
-
725052
addition of the enzyme to an aerobic buffer, 50 mM Tris/HCl, pH 7.6 results in a 98% loss of activity within 15 min, presence of CO has no apparent effect on the stability of the enzyme
-
390452
enzymatic activity is destroyed by air, a low amount of activity still is present after 2 h exposure to air
-
390454
extreme oxygen lability
extremely oxygen-labile, even in N2 atmosphere with less than 5 ppm O2 the pure enzyme loses a significant amount of its activity within 18 h, 2 mM dithionite protects from inactivation
-
390450
extremely sensitive to air, most of the enzyme activity is lost upon exposure to air for 1 min, longer incubation results in complete inactivation
-
390449
oxygen stable, 10% loss in activity after 72 h exposure to air at 4°C
-
390473
Oxygen treatment results in an activity loss of 90% within 30 min. Treatment of oxygen-inactivated enzyme with CO, H2, or dithionite does not restore activity
-
727713
strong inhibition by oxygen, extremely sensitive, exposed to air activity is lost in less than 1 min
-
390449
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 5°C, 50 mM Tris/HCl, pH 7.5, 2 mM sodium dithionite, 0.2 mM methyl viologen, 50% v/v glycerol, stable for more than 1 month
-
-20°C, stored frozen in an oxygen-free atmosphere in buffer containing glycerol and 2 mM dithionite, not stable for more than 1 month
-
-70°C, samples thawed under anaerobic conditions exhibits full activity even after 6 months of storage
-
5°C, stored in an oxygen-free atmosphere in buffer containing glycerol and 2 mM dithionite, not stable for more than 1 month
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cosmogel His-Accept column chromatography, and gel filtration
-
Q-Sepharose column chromatography and Sephacryl S-300 gel filtration
-
Q-Sepharose column chromatography, CHT-I column chromatography, and Superdex 200 gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DH5 alpha cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the synthesis of CO-DH is induced in the presence of CO. The CutR protein is involved in the induction of CO-DH synthesis in the presence of CO. When the wild type strain grown on 0.2% (w/v) glucose is further grown on 0.002% (w/v) glucose for 5 h, the CO-DH activity is increased by 1.6fold relative to that detected in the same strain grown on 0.2% (w/v) glucose for additional 5 h as a control
the synthesis of CO-DH is induced in the presence of CO. The CutR protein is involved in the induction of CO-DH synthesis in the presence of CO. When the wild type strain grown on 0.2% (w/v) glucose is further grown on 0.002% (w/v) glucose for 5 h, the CO-DH activity is increased by 1.6fold relative to that detected in the same strain grown on 0.2% (w/v) glucose for additional 5 h as a control
-
the synthesis of CO-DH is induced in the presence of CO. The CutR protein is involved in the induction of CO-DH synthesis in the presence of CO. When the wild type strain grown on 0.2% (w/v) glucose is further grown on 0.002% (w/v) glucose for 5 h, the CO-DH activity is increased by 1.6fold relative to that detected in the same strain grown on 0.2% (w/v) glucose for additional 5 h as a control
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A110C
A219F
-
mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
A222L
A265M
-
mutation within tunnel region of alpha subunit, absence of strong cooperative inhibition of CO, little synthesis of acetyl-CoA
A578C
-
mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
F70W
-
mutant designed to block region that connects the CO tunnel at the betabeta interface with a water channel, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
H113A
-
44% of wild type activity, in presence of imidazole, 45% of wild type activity
H116A
-
6% of wild type activity, in presence of imidazole, 3% of wild type activity
L215F
-
mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
N101Q
-
mutant designed to block region that connects the CO tunnel at the betabeta interface with a water channel, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
C338A
-
complete loss of activity. Unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C451A
-
complete loss of activity. Unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C451S
-
1.4% of wild-type specific activity. Unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C481A
-
unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
H265V
-
no CO oxidation activity in presence or absence of nickel, production of formate at same level as wild type
additional information
A110C
-
mutation within tunnel region of alpha subunit, absence of strong cooperative inhibition of CO, no synthesis of acetyl-CoA
A110C
-
alpha subunit mutant enzyme showing electron paramagnetic resonance spectrum after Ni-activation
A222L
-
mutation within tunnel region of alpha subunit, absence of strong cooperative inhibition of CO, no synthesis of acetyl-CoA
A222L
-
alpha subunit mutant enzyme showing electron paramagnetic resonance spectrum after Ni-activation
additional information
-
more than threefold induction of enzyme activity and increase in enzyme expression, as well as pyruvate oxidoreductase activity and expression, in a mutant lacking the membrane-bound energy-conserving hydrogenase Ehb
additional information
D5G1Y2; D5G1Y0; D5G1Y1;
the mutant YK002 does not produce the large subunit of CO-DH and exhibits no CO-DH activity
additional information
-
the mutant YK002 does not produce the large subunit of CO-DH and exhibits no CO-DH activity
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
assay method for enzyme in complex with protein CooF which mediates electron transfer from enzyme to the CO-induced hydrogenase based on membranes containing high levels of CO-induced hydrogenase
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