Information on EC 1.2.99.2 - carbon-monoxide dehydrogenase (acceptor)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
1.2.99.2
-
RECOMMENDED NAME
GeneOntology No.
carbon-monoxide dehydrogenase (acceptor)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
CO + H2O + A = CO2 + AH2
show the reaction diagram
CO may react with OH- rather than with H2O
-
CO + H2O + A = CO2 + AH2
show the reaction diagram
ping-pong mechanism
-
CO + H2O + A = CO2 + AH2
show the reaction diagram
ping-pong mechanism
-
CO + H2O + A = CO2 + AH2
show the reaction diagram
enzyme also catalyzes acetyl-CoA/CoA and acetyl-CoA/CO exchange reaction, enzyme has both CO-dehydrogenase and acetyl-CoA synthase activity
-
CO + H2O + A = CO2 + AH2
show the reaction diagram
kinetics, oxidation state of Fe-S cluster during catalysis
-
CO + H2O + A = CO2 + AH2
show the reaction diagram
mechanism, CO binding labilizes the hydroxyl bridging Ni and Fe and increases the nucleophilic tendency toward attacking Ni-bound carbonyl
-
CO + H2O + A = CO2 + AH2
show the reaction diagram
mechanism, enzyme is capable of producing formate
-
CO + H2O + A = CO2 + AH2
show the reaction diagram
CO2/CO tunnel gating mechanism
-
CO + H2O + A = CO2 + AH2
show the reaction diagram
mechnaism via thiocarbonate-like intermediate state
-
CO + H2O + A = CO2 + AH2
show the reaction diagram
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 + A = CO2 + AH2
show the reaction diagram
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 + A = CO2 + AH2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Carbon fixation pathways in prokaryotes
-
carbon monoxide dehydrogenase complex
-
carbon tetrachloride degradation II
-
hydrogen production VI
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
Nitrotoluene degradation
-
SYSTEMATIC NAME
IUBMB Comments
carbon-monoxide:acceptor oxidoreductase
Contains a [Ni3Fe-4S] cluster and [4Fe-4S] clusters. It uses many electron acceptors, including ferredoxin, methyl viologen and benzyl viologen and flavins, but not pyridine nucleotides. Forms part of a membrane-bound multienzyme complex with EC 1.12.99.6, hydrogenase (acceptor), which catalyses the overall reaction: CO + H2O = CO2 + H2.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetyl coenzyme A synthase/carbon monoxide dehydrogenase
-
-
acetyl-CoA synthase/carbon monoxide dehydrogenase
-
bifunctional enzyme
ACS/CODH
-
bifunctional enzyme
ACS/CODH
-
bifunctional enzyme with ACS alpha subunits and CODH beta subunits
Carbon dioxide/carbon monoxide oxidoreductase
-
-
-
-
Carbon monoxide dehydrogenase
-
-
-
-
carbon monoxide dehydrogenase-corrinoid enzyme complex
-
-
-
-
carbon monoxide dehydrogenase/acetyl-CoA synthase
-
bifunctional enzyme
carbon monoxide dehydrogenase/acetyl-CoA synthase
P27989
bifunctional enzyme
Carbon monoxide oxidoreductase
-
-
-
-
Cdh
-
-
-
-
CO dehydrogenase
-
-
-
-
CO dehydrogenase
-
-
CO dehydrogenase
Mycobacterium sp. JC1, Mycobacterium sp. JC1 DSM 3803
-
-
-
CO dehydrogenase
P19919 and P19920 and P19921
-
CO dehydrogenase complex
-
-
CO dehydrogenase complex II
-
-
CO dehydrogenase II
-
-
CO dehydrogenase/acetyl-CoA synthase
-
-
-
-
Co-DG
-
-
-
-
CO-DH
-
; possesses also nitric oxid dehydrogenase activity in mycobacteria
CO-DH
D5G1Y2 and D5G1Y0 and D5G1Y1
-
CO-DH
Mycobacterium sp. JC1
-
-, possesses also nitric oxid dehydrogenase activity in mycobacteria
-
CO-DH
Mycobacterium sp. JC1 DSM 3803
-, D5G1Y2 and D5G1Y0 and D5G1Y1
-
-
CO-DH
-
; possesses also nitric oxid dehydrogenase activity in mycobacteria
CODH
-
-
-
-
CODH
Aeropyrum pernix TB5
-
-
-
CODH
Q7X0G3
-
CODH
-
beta subunit of the bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase complex
CODH
-
beta subunit of the bifunctional acetyl coenzyme A synthase/carbon monoxide dehydrogenase complex
CODH
-
forms a complex with acetyl-CoA synthase
CODH
P19919 and P19920 and P19921
-
CODH
Oligotropha carboxidovorans ATCC 49405
P19919 and P19920 and P19921
-
-
CODH
Stappia carboxidovorans
-
-
CODH
A1E2F7
-
CODH
Stappia sp.
Q7X0G5, Q7X0G6, Q7X0G8, Q7X0G9
-
CODH
Q7X0G5, Q7X0G6, Q7X0G8, Q7X0G9
-
-
CODH
Q7X0G2
-
CODH
F5YMN6, F8TH35
-
CODH
F8TH35
-
-
CODH
F5YMN6
-
-
CODH
F8TH37, F8TH38, F8TH39
-
CODH
F8TH37
-
-
CODH
F8TH38
-
-
CODH
F8TH39
-
-
CODH II
Carboxydothermus hydrogenoformans Z2901 (DSM6008)
Q9F8A8
-
-
CODH/ACS
-
; bifunctional enzyme carbon monoxide dehydrogenase/acetyl-CoA synthase
CODH/ACS
P27989
bifunctional enzyme
CODHACS
-
bifunctional enzyme, CODHACS is a macromolecular machine that catalyzes the last step of the Wood-Ljungdahl pathway of anaerobic carbon dioxide fixation
coos
F5YDA7
gene encoding the catalytic (beta) subunit of the anaerobic CODH enzyme complex
coos
F5YDA7
gene encoding the catalytic (beta) subunit of the anaerobic CODH enzyme complex
-
coos
F5YMN6, F8TH35
gene encoding the catalytic (beta) subunit of the anaerobic CODH enzyme complex
coos
F8TH35
gene encoding the catalytic (beta) subunit of the anaerobic CODH enzyme complex
-
coos
F5YMN6
gene encoding the catalytic (beta) subunit of the anaerobic CODH enzyme complex
-
coos
F8TH37, F8TH38, F8TH39
gene encoding the catalytic (beta) subunit of the anaerobic CODH enzyme complex
coos
F8TH37
gene encoding the catalytic (beta) subunit of the anaerobic CODH enzyme complex
-
coos
F8TH38
gene encoding the catalytic (beta) subunit of the anaerobic CODH enzyme complex
-
coos
F8TH39
gene encoding the catalytic (beta) subunit of the anaerobic CODH enzyme complex
-
Dehydrogenase, carbon monoxide
-
-
-
-
Ni,Fe-dependent carbon monoxide dehydrogenase
-
-
Ni-Fe carbon monoxide dehydrogenase II
-
-
Ni-Fe carbon monoxide dehydrogenase II
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
64972-88-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Aeropyrum pernix TB5
-
-
-
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
Archaeoglobus lithotrophicus TF-2
-
-
-
Manually annotated by BRENDA team
Autotrophic methanogenic bacterium
-
-
-
Manually annotated by BRENDA team
gram-negativ soil bacterium
-
-
Manually annotated by BRENDA team
enzyme CooS in complex with an electron transfer protein CooF and a membrane bound [Ni-Fe] hydrogenase
-
-
Manually annotated by BRENDA team
hydrogenogenic bacterium
-
-
Manually annotated by BRENDA team
strain Z-2901 (DSM 6008)
-
-
Manually annotated by BRENDA team
strain Z-2901 (DSM 6008)
-
-
Manually annotated by BRENDA team
Carboxydothermus hydrogenoformans Z2901 (DSM6008)
-
Uniprot
Manually annotated by BRENDA team
chemolithoautotrophic
-
-
Manually annotated by BRENDA team
chemolithoautotrophic
-
-
Manually annotated by BRENDA team
large subunit, fragment; synonym Stappia aggregata
UniProt
Manually annotated by BRENDA team
more than threefold induction of enzyme activity and increase in enzyme expression in a mutant lacking the membrane-bound energy-conserving hydrogenase Ehb
-
-
Manually annotated by BRENDA team
strain DSM 521
-
-
Manually annotated by BRENDA team
bifunctional acetyl-coenzyme A synthase/carbon monoxide dehydrogenase, isolated alpha subunit
-
-
Manually annotated by BRENDA team
bifunctional enzyme with carbon-monoxide dehydrogenase/acetyl coenzyme A synthase activity
-
-
Manually annotated by BRENDA team
CODH/ACS subunit beta; formerly Clostridium thermoaceticum strain ATCC 39073
UniProt
Manually annotated by BRENDA team
formerly Clostridium thermoaceticum strain ATCC 39073
-
-
Manually annotated by BRENDA team
strain DSM 521
-
-
Manually annotated by BRENDA team
large, medium and small subunit
D5G1Y2 and D5G1Y0 and D5G1Y1
UniProt
Manually annotated by BRENDA team
strain JC1; strain JC1 DSM 3803
-
-
Manually annotated by BRENDA team
Mycobacterium sp. JC1
strain JC1; strain JC1 DSM 3803
-
-
Manually annotated by BRENDA team
Mycobacterium sp. JC1 DSM 3803
-
-
-
Manually annotated by BRENDA team
Mycobacterium sp. JC1 DSM 3803
large, medium and small subunit
D5G1Y2 and D5G1Y0 and D5G1Y1
UniProt
Manually annotated by BRENDA team
strain H37Ra; strain H37Ra ATCC 35835
-
-
Manually annotated by BRENDA team
strain ATCC 15483
-
-
Manually annotated by BRENDA team
no activity in heterotrophic methanogenic bacteria
-
-
-
Manually annotated by BRENDA team
no activity in Methanobrevibacter ruminantium
-
-
-
Manually annotated by BRENDA team
no activity in Methanobrevibacter smithii
-
-
-
Manually annotated by BRENDA team
no activity in Methanococcus voltae
-
-
-
Manually annotated by BRENDA team
no activity in Methanospirillum hungatei
-
-
-
Manually annotated by BRENDA team
P19919 large subunit, P19920 medium subunit, P19921 small subunit
P19919 and P19920 and P19921
UniProt
Manually annotated by BRENDA team
Oligotropha carboxidovorans ATCC 49405
P19919 large subunit, P19920 medium subunit, P19921 small subunit
P19919 and P19920 and P19921
UniProt
Manually annotated by BRENDA team
purple nonsulfur bacterium, the enzyme exists in the forms, I and II, which differ in metal content
-
-
Manually annotated by BRENDA team
Stappia carboxidovorans
-
-
-
Manually annotated by BRENDA team
large subunit, fragment
UniProt
Manually annotated by BRENDA team
large subunit, fragment
UniProt
Manually annotated by BRENDA team
Stappia sp.
large subunit, fragment; strain KB812
UniProt
Manually annotated by BRENDA team
Stappia sp.
large subunit, fragment; strain KB902
UniProt
Manually annotated by BRENDA team
Stappia sp.
large subunit, fragment; strain M4
UniProt
Manually annotated by BRENDA team
Stappia sp.
large subunit, fragment; strain M8
UniProt
Manually annotated by BRENDA team
large subunit, fragment; strain KB812
UniProt
Manually annotated by BRENDA team
large subunit, fragment; strain KB902
UniProt
Manually annotated by BRENDA team
large subunit, fragment; strain M4
UniProt
Manually annotated by BRENDA team
large subunit, fragment; strain M8
UniProt
Manually annotated by BRENDA team
large subunit, fragment
UniProt
Manually annotated by BRENDA team
analogue of the C-cluster of Carboxydothermus hydrogenoformans
-
-
Manually annotated by BRENDA team
grows on acetate if cocultured with hydrogen-consuming methanogenic partner Methanothermobacter thermautrophicus
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Archaeoglobus lithotrophicus TF-2, Ferroglobus placidus DSM 10642
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CO + ferredoxin
?
show the reaction diagram
-
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
CO2 + H2
show the reaction diagram
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
-
-
-
-
r
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
P27989
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
D5G1Y2 and D5G1Y0 and D5G1Y1
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
P19919 and P19920 and P19921
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor + H+
show the reaction diagram
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
Oligotropha carboxidovorans ATCC 49405
P19919 and P19920 and P19921
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
Mycobacterium sp. JC1 DSM 3803
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
Mycobacterium sp. JC1 DSM 3803
D5G1Y2 and D5G1Y0 and D5G1Y1
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
Carboxydothermus hydrogenoformans Z2901 (DSM6008)
Q9F8A8
-
-
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
-
-
-
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the enzyme is involved in the Wood pathway of acetyl-CoA synthesis
-
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
key enzyme in C1-pathway of acetyl-CoA degradation
-
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
-
the formation of acetyl-CoA from methyltetrahydrofolate requires several enzymes, including CO dehydrogenase
-
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
-
ferredoxin and a membrane-bound b-type cytochrome are considered to be the native electron carriers
-
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
-
catalyzes the final step in the synthesis of acetyl-CoA
-
-
-
CO + H2O + electron acceptor
?
show the reaction diagram
-
catalyzes the final step in the synthesis of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
-
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
?
show the reaction diagram
-
enzyme may also be involved in the formation of acetyl-CoA from methanol in methanogens
-
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
-
key role of the enzyme in the synthesis of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
CO2 + reduced electron acceptor
show the reaction diagram
-
a proton gradient across the cytoplasmic membrane is generated by channeling the electrons formed via cytochrome b561 into a CO-insensitive respiratory chain
-
?
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
the medium subunit contains FAD
flavin adenine dinucleotide
-
suggested from gene sequence analysis
flavin adenine dinucleotide
-
-
flavin adenine dinucleotide
-
cofactor is released upon treatment with guanidine-HCl, SDS, heat or acid
flavin adenine dinucleotide
-
1.99 mol flavin/mol enzyme
iron-sulfur centre
-
-
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
Molybdopterin cytosine dinucleotide
-
-
Molybdopterin cytosine dinucleotide
-
-
Ni-4Fe-5S center
-
active site cluster
Ni-Fe-4S center
-
active site called the C-cluster
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
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
copper
-
contains copper, essential for activity
Cu2+
-
the enzyme contains copper
Cu2+
-
the native enzyme contains copper in the active site
Fe2+
-
contains 9 Fe+ per monomer
Fe2+
-
contains one Ni-4Fe-5S cluster
Fe2+
-
contains a [NiFe4S5] center called cluster C; Ni-, Fe-, and S-containing metal center called cluster C
Fe2+
P27989
contains iron
Fe2+
-
the enzyme contains iron
Fe2+
-
CODHII contains iron, the active site of CODH contains a [NiFe4S4OHx] cluster known as C-cluster
Iron
-
enzyme form I contains 7 iron and 6 sulfur per monomer; enzyme form II contains 9 iron and 8 sulfur per monomer
Iron
-
contains 15.6 mol of iron per mol of alpha2beta oligomer
Iron
-
the alphabeta dimer contains approximately 9-11 mol of iron and 12-14 mol of acid-labile sulfur per mol of dimer
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
-
contains 25 mol of Fe2+ and 20 mol of S2- per mol of tetramer, the enzyme contains 2 (4Fe-4S)+ clusters
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
-
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
-
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
-
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
Iron
-
Fe-S cluster
Iron
-
61.5 mol nonheme iron per mol of complex
Iron
-
[Ni-4Fe-4S] cluster or [Ni-4Fe-5S] cluster
Iron
-
4Fe-4S cluster
Iron
-
wild-type, 8.97 mol per mol of enzyme
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
-
2.29 mol/mol enzyme
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
Molybdenum
-
the enzyme contains molybdenum
Ni-Fe-S center
-
-
Ni2+
-
contains Ni2+-activated alpha subunits, Ni2+ is required for activity and oligomerization
Ni2+
-
contains 0.1 Ni2+ per monomer
Ni2+
-
contains one Ni-4Fe-5S cluster
Ni2+
-
activates
Ni2+
-
contains a [NiFe4S5] center called cluster C; Ni-, Fe-, and S-containing metal center called cluster C
Ni2+
P27989
contains nickel
Ni2+
-
CODHII contains nickel, the active site of CODH contains a [NiFe4S4OHx] cluster known as C-cluster
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
-
contains 1.3 mol of nickel per mol of alpha2beta2 oligomer
Nickel
-
contains 2 g-atoms of nickel per mol of enzyme
Nickel
-
the alphabeta dimer contains approximately 2 mol of nickel per mol of dimer
Nickel
-
contains 2 mol of nickel per mol of alphabeta dimer
Nickel
-
contains 2-3 mol of nickel per mol of enzyme
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
-
contains 1.3 mol of Ni2+ per mol of tetramer
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
-
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
-
carbon monoxide dehydrogenase II, enzyme contains 5 metal clusters, a [Ni-4Fe-5S] cluster appears to be the active site of CO oxidation
Nickel
-
3 mol per mol of complex
Nickel
-
[Ni-4Fe-4S] cluster or [Ni-4Fe-5S] cluster
Nickel
-
Ni-depleted enzyme is still able to produce formate
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
Nickel
-
wild-type, 0.85 mol per mol of enzyme. Analysis of activation of wild-type and mutant apo-enzymes by nickel
S2-
-
contains a [NiFe4S5] center called cluster C
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
Zinc
-
the alphabeta dimer contains approximately 1 mol of zinc per mol of dimer
Zinc
-
contains 1 mol of zinc per mol of alphabeta dimer
[2Fe-2S]-center
-
the small subunit contains two [2Fe-2S] centers
Molybdenum
-
contains molybdenum, essential for activity
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+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
1 mM, inactivates CO/acetyl-CoA exchange activity completely but has no effect on CO oxidation
2,3-Butanedione
-
-
CN-
-
0.04 mM, 60% inhibition within 10 s, CO reverses inhibition
CN-
-
KCN, reversible
CN-
-
CO and COS protect from inhibition; CO, CO2 and COS reverse inhibition
CN-
-
CO, CO2 and COS reverse inhibition; dithionite slows the inhibition, but cannot reactivate the enzyme
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-
-
1.2 mM, 98% inhibition of acetyl-CoA/CoA exchange reaction
CN-
-
binds directly to the C-cluster
CO
-
inhibition of the exchange reaction between acetyl-CoA and CoA
CO
-
45% CO in headspace, 50% inhibition
CO
-
weak, isolated alpha subunit
COS
-
rapid-equilibrium inhibitor largely competitive versus CO, uncompetitive versus methyl viologen
cyanide
-
potent inhibitor
cyanide
-
inhibitory at 5 mM; strong competitive inhibitor
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 70C 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
cyanide
-
slow binding inhibitor of CODH
D-glucose
Q7X0G3
partially inhibited by incubation with 0.5 mM exogenous D-glucose
dephospho-CoASH
-
-
Glyoxaldehyde
-
inactivation requires enzymatic turnover
N2O
-
inhibition of the exchange reaction between acetyl-CoA and CoA
pivaloylpantetheine-SH
-
-
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
SCN-
-
binds to C-center, mixed partial inhibition
Methyl iodide
-
CO promotes inhibition
additional information
-
not inhibited by 20 mM formaldehyde or acetaldehyde
-
additional information
-
not inhibited by propyl iodide, methyl iodide, carbon tetrachloride, EDTA or nitrilotriacetate
-
additional information
-
inhibition data are interpreted in terms of two binding sites for CO on CO dehydrogenase
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.5
-
2,3,5-triphenyltetrazolium chloride
-
below 0.5 mM
0.6
-
acetyl-CoA
-
CO/acetyl-CoA exchange reaction
1.5
-
acetyl-CoA
-
acetyl-CoA/CoA exchange reaction
0.01
-
CO
-
CO/acetyl-CoA exchange reaction
0.024
-
CO
-
mutant C451S, pH 7.5
0.03
-
CO
-
25C, isolated alpha subunit
0.032
-
CO
-
wild-type, pH 7.5
0.098
-
CO
-
at 10C
0.05
-
CoA
-
acetyl-CoA/CoA exchange reaction
0.008
-
Ferredoxin
-
-
-
0.065
-
methyl viologen
-
-
0.12
-
methyl viologen
-
-
1.4
-
methyl viologen
-
-
3.03
-
methyl viologen
-
50C, pH 8.4
4
-
methyl viologen
-
at 70C
7.1
-
methyl viologen
-
-
0.00295
-
methylene blue
-
Ag+-substituted enzyme, at pH 7.0 and 25C
0.0107
-
methylene blue
-
native enzyme, at pH 7.0 and 25C
0.0107
-
methylene blue
-
at pH 7.2 and 25C
5
-
propionyl-CoA
-
-
1.7
-
Trichloroethylene
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.17
-
CO
-
turnover mumber for CO/CO2 exchange reaction
7.33
-
CO
-
acetyl-CoA/CO exchange reaction
11
-
CO
-
25C, isolated alpha subunit
13
-
CO
-
CO oxidation, 50C, pH 5.3, electron acceptor ferredoxin II
22
-
CO
-
CO oxidation, at 1C
600
-
CO
-
CO oxidation, at 55C, pH 7.6
3250
-
CO
-
CO oxidation, extrapolated maximum value at 55C, pH 10.8
8.2
-
methylene blue
-
Ag+-substituted enzyme, at pH 7.2 and 25C
57.8
-
methylene blue
-
at pH 7.2 and 25C
93.3
-
methylene blue
-
native enzyme, at pH 7.2 and 25C
additional information
-
additional information
-
42000/min/Ni, substrate methyl viologen
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2780
-
methylene blue
-
Ag+-substituted enzyme, at pH 7.2 and 25C
13111
8700
-
methylene blue
-
native enzyme, at pH 7.2 and 25C
13111
8700
-
methylene blue
-
at pH 7.2 and 25C
13111
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.45
-
Butyryl-CoA
-
inhbition of CO/acetyl-CoA exchange reaction
0.4
-
CO
-
noncompetitive inhibition of the acetyl-CoA exchange reaction
0.4
-
CO
-
inhibition of acetyl-CoA/CoA exchange reaction
0.007
-
CoASH
-
inhbition of CO/acetyl-CoA exchange reaction
0.0023
-
COS
-
competitive inhibition vs. CO
0.0158
-
COS
-
noncompetitive inhibition vs. methyl viologen
1.4
-
crotonyl-CoA
-
inhbition of CO/acetyl-CoA exchange reaction
0.0217
-
cyanide
-
at 23C, in 4 mM dithionite, and 4 mM dithiothreitol
0.035
-
dephospho-CoASH
-
inhbition of CO/acetyl-CoA exchange reaction
6
-
desulfo-CoA
-
inhbition of CO/acetyl-CoA exchange reaction
1.2
-
pivaloylpantetheine-SH
-
inhbition of CO/acetyl-CoA exchange reaction
1.3
-
propionyl-CoA
-
inhbition of CO/acetyl-CoA exchange reaction
16
-
SCN
-
assay at pH 5.5, Ki depends on pH and temperature
830
-
SCN
-
assay at pH 10.7, Ki depends on pH and temperature
0.00004
-
Sulfide
-
pH 7.5, 30C
-
0.00006
-
Sulfide
-
pH 7.5, 30C
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
both for enzyme and complex
6.7
-
-
in cell-free extracts
7.5
-
-
assay at
8.4
-
-
mutant C451S
8.6
-
-
wild-type
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
8
-
-
about 60% of activity at pH 9.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
65
-
-
assay at
80
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
75
100
-
about 65% activity at 75C, about 75% activity at 80C, about 80% activity at 85C, about 90% activity at 90C, 100% activity at 95C, about 30% activity at 100C, respectively
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17390
-
D5G1Y2 and D5G1Y0 and D5G1Y1
small subunit, calculated from sequence of cDNA
30620
-
D5G1Y2 and D5G1Y0 and D5G1Y1
medium subunit, calculated from sequence of cDNA
61600
-
-
gel filtration
72000
-
-
beta subunit, SDS-PAGE
85970
-
D5G1Y2 and D5G1Y0 and D5G1Y1
large subunit, calculated from sequence of cDNA
120000
-
-
gel filtration, enzyme
161000
-
-
dialyzed enzyme, gel filtration
163700
-
-
calculated from amino acid sequence
190000
-
-
gel filtration
210000
-
-
gel filtration
220000
-
-
nondenaturing PAGE
230000
-
-
native PAGE
235000
-
-
gel filtration
250000
-
-
gradient gel electrophoresis
273500
-
-
deduced from amino acid sequence
300000
-
-
sedimentation equilibrium ultracentrifugation
410000
-
-
gel filtration
436000
-
-
gel filtration
450000
-
-
gel filtration, complex
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
-
-
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
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 70000, SDS-PAGE
?
Carboxydothermus hydrogenoformans Z2901 (DSM6008)
-
x * 70000, SDS-PAGE
-
dimer
-
2 * 62000, SDS-PAGE, enzyme
heterohexamer
Oligotropha carboxidovorans ATCC 49405
-
-
-
heterotetramer
-
x-ray crystallography
heterotetramer
-
1 * 86600 + 2 * 34500 + 1 * 12600, SDS-PAGE
heterotetramer
Aeropyrum pernix TB5
-
1 * 86600 + 2 * 34500 + 1 * 12600, SDS-PAGE
-
hexamer
-
3 * 71000, beta, + 3 * 78000, alpha, 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
hexamer
-
L2,M2,S2, 2 * 87224 + 2 * 30694 + 2 * 17752, deduced from gene sequence, SDS-PAGE
hexamer
-
L2,M2,S2, 2 * 75000 + 2 * 28400 + 2 * 17200, SDS-PAGE
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
-
2 * 19700 + 2 * 84500, alpha2beta2, SDS-PAGE
tetramer
-
2 * 21000 + 2 * 89000, SDS-PAGE
tetramer
-
2 * 19000 + 2 * 94000, alpha2beta2, SDS-PAGE
tetramer
-
2 * 19400 + 2 * 79400, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 82000 + 2 * 73000, enzyme previously thought to have an alpha3,beta3 structure, SDS-PAGE
monomer
-
1 * 61800, SDS-PAGE
additional information
-
properties of enzyme in complex with protein CooF which mediates electron transfer from enzyme to the CO-induced hydrogenase
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
native and cyanide bound CODH/ACS complex
P27989
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9.5
-
wild-type and mutants apo-enzymes, stable for at least 30 min within this range
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24
-
-
10 min, about 30% loss of activity in presence of CO, stable in absence of CO
39
-
-
10 min, 45% loss of activity in presence of CO, stable in absence of CO
60
-
-
10 min, about 10% loss of activity
62
-
-
10 min, about 65% loss of activity in presence of CO, about 5% loss of activity in absence of CO
72
-
-
10 min, complete inactivation
80
-
-
10 min, about 85% loss of activity in presence of CO, about 20% loss of activity in absence 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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
CN- inactivates
-
72 h exposure to air at 4C, about 10% loss of activity
-
CO renders the enzyme more susceptible to temperature inactivation
-
98% loss of activity after 15 min in an aerobic buffer
-
the presence of CO has no apparent effect on the stability
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
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
oxygen stable, 10% loss in activity after 72 h exposure to air at 4C
-
390473
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
extreme oxygen lability
-
390456
extreme oxygen lability
-
390452, 390453
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 1 month, 100% inactivation
-
-20C or 5C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Q-Sepharose column chromatography, CHT-I column chromatography, and Superdex 200 gel filtration
-
anion-exchange, hydrophobic interaction, gel filtration
-
carbon monoxide dehydrogenase II
-
Cosmogel His-Accept column chromatography, and gel filtration
-
Ni-NTA agarose column chromatography
-
Q-Sepharose column chromatography and Sephacryl S-300 gel filtration
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
Mycobacterium sp. JC1 DSM 3803
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C56A
-
devoid of CO oxidation activity
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
A121H/H122A
-
11% of wild type activity
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
-
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
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
C316S
-
0.3% of wild type activity
E115H/H116A
-
24% of wild type activity
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
H113A/H116A/H119A
-
no activity
H113A/H119A
-
15% of wild type activity
H116A
-
6% of wild type activity, in presence of imidazole, 3% of wild type activity
H116A/G117H
-
0.8% of wild type activity
H116C
-
46% of wild type activity
H116D
-
0.4% of wild type activity
H119A
-
27% of wild type activity
H122A
-
3% of wild type activity
H122A/A123H
-
72% of wild type activity
K587A
-
42% of wild type activity
K587A/H113A
-
0.7% 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
N284A
-
41% of wild type activity
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+
C531A
-
0.1% of wild-type specific activity
H265V
-
no CO oxidation activity in presence or absence of nickel, production of formate at same level as wild type
K563L
-
very low CO oxidation activity
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
N284A/H119A
-
36% of wild type activity
additional information
D5G1Y2 and D5G1Y0 and D5G1Y1
the mutant YK002 does not produce the large subunit of CO-DH and exhibits no CO-DH activity
additional information
Mycobacterium sp. JC1 DSM 3803
-
the mutant YK002 does not produce the large subunit of CO-DH and exhibits no CO-DH activity
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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