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Enzyme Nomenclature
Information on EC 1.2.2.4 - carbon-monoxide dehydrogenase (cytochrome b-561)
for references in articles please use BRENDA:EC1.2.2.4
Word Map on EC 1.2.2.4
- 1.2.2.4
- co2
-
codhs
- nickel
- thermoaceticum
- rubrum
-
acetogenic
- rhodospirillum
- methanosarcina
- oligotropha
- hydrogenoformans
-
methanogenesis
-
sulfate-reducing
-
c-clusters
- carboxidovorans
- corrinoids
- carboxydothermus
-
co-dependent
- cubane
-
co-oxidizing
-
nickel-containing
-
ni-containing
-
acetate-grown
- barkeri
-
wood-ljungdahl
-
carboxydotrophic
-
methyl-coenzyme
-
homoacetogenic
- acetobacterium
-
molybdenum-containing
- moorella
-
acetogenesis
-
cubane-type
- methyltetrahydrofolate
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.2.2.4
-
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RECOMMENDED NAME
GeneOntology No.
carbon-monoxide dehydrogenase (cytochrome b-561)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561
-
-
-
-
CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561
mechanism, necessity of S-selanyl-cysteine for catalysis
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
carbon monoxide,water:cytochrome b-561 oxidoreductase
Contains molybdopterin cytosine dinucleotide, FAD and [2Fe-2S]-clusters. Oxygen, methylene blue and iodonitrotetrazolium chloride can act as nonphysiological electron acceptors.
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CAS REGISTRY NUMBER
COMMENTARY
64972-88-9
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
Fe3+-EDTA + H2O + ferrocytochrome b-561
Fe2+-EDTA + H+ + ferricytochrome b-561
-
-
-
-
?
potassium ferricyanide + H2O + ferrocytochrome b-561
potassium ferrocyanide + H+ + ferricytochrome b-561
-
-
-
-
?
CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
-
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
-
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
-
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
-
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
-
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
-
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
-
-
-
?
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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 + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
-
the only enzyme involved in CO oxidation by carboxydotrophic bacteria
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
contains 2 mol of non-covalently bound FAD per mol of enzyme
FAD
-
contains 2 mol of non-covalently bound FAD per mol of enzyme
molybdenum cofactor
-
the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
molybdenum cofactor
-
the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
molybdenum cofactor
-
the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
molybdenum cofactor
-
the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
molybdenum cofactor
-
the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Mo5+
-
1.9 mol per mol of enzyme dimer, a 1:1 mononuclear complex of molybdopterin-cytosine dinucleotide and the Mo ion
Mo6+
functions in the proper orientation of the catalytically active residues C385 and E757, crystalization data
Molybdenum
[2Fe-2S]-center
-
6.9 mol per mol of enzyme dimer, type I and type II [2Fe-2S]-centers
additional information
-
the reconstitution reaction of the solubilized enzyme with depleted membranes requires cations with effectiveness that increases with increasing ionic charge: Li+, Mg2+, Mn2+, Cr3+, La3+
Iron
-
enzyme contains 8 mol of Fe and 8 mol of acid-labile sulfide groups per mol of enzyme
Iron
-
enzyme contains 2 different types of Fe2S2 centers; enzyme contains 8 mol of Fe and 8 mol of acid-labile sulfide groups per mol of enzyme
Iron
-
enzyme contains 2 different types of Fe2S2 centers; enzyme contains 8 mol of Fe and 8 mol of acid-labile sulfide groups per mol of enzyme
Molybdenum
-
enzyme contains Mo; the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
Molybdenum
-
enzyme contains 2 mol of Mo per mol of enzyme; the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
Molybdenum
-
enzyme contains 2 mol of Mo per mol of enzyme; the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
Molybdenum
-
the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
Molybdenum
-
enzyme contains Mo; the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the portion of enzyme localized in the cytoplasm is low during exponential growth and high in stationary cells
-
a weakly-bound pool and a tightly-bound pool of the enzyme
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17000
17750
-
x * 87200, molybdopterin binding subunit L, + x * 30700, FAD-binding subunit M, + x * 17750, subunit S with two [2Fe-2S]-center binding sites, deduced from gene sequence
17800
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
30200
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
30700
-
x * 87200, molybdopterin binding subunit L, + x * 30700, FAD-binding subunit M, + x * 17750, subunit S with two [2Fe-2S]-center binding sites, deduced from gene sequence
33000
70000
87200
-
x * 87200, molybdopterin binding subunit L, + x * 30700, FAD-binding subunit M, + x * 17750, subunit S with two [2Fe-2S]-center binding sites, deduced from gene sequence
88700
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
230000
-
sucrose density gradient centrifugation, sedimentation equilibrium experiments, gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 87200, molybdopterin binding subunit L, + x * 30700, FAD-binding subunit M, + x * 17750, subunit S with two [2Fe-2S]-center binding sites, deduced from gene sequence
heterohexamer
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
hexamer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molybdoironflavoprotein
additional information
R384 has a gamma-hydroxy modification, C385 carries the catalytically essential S-selanyl-group
molybdoironflavoprotein
-
molybdenum with three oxygen ligands, molybdopterin-cytosine dinucleotide and S-selanylcysteine at active site
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Chromaffin granule cytochrome b-561 could partially restore the wild-type phenotype; expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Duodenal cytochrome b-561 could partially restore the wild-type phenotype; expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Lysosomal cytochrome b-561 could partially restore the wild-type phenotype
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R67A
-
incative, domain predicted to bind ascorbate at the electron-accepting site of the protein
Y66A
-
incative, domain predicted to bind ascorbate at the electron-accepting site of the protein
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.2.4)
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