Information on EC 1.2.2.4 - carbon-monoxide dehydrogenase (cytochrome b-561)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

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EC NUMBER
COMMENTARY hide
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 hide
ORGANISM
UNIPROT
LITERATURE
CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
64972-88-9
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
show the reaction diagram
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
show the reaction diagram
Fe3+-EDTA + H2O + ferrocytochrome b-561
Fe2+-EDTA + H+ + ferricytochrome b-561
show the reaction diagram
-
-
-
-
?
potassium ferricyanide + H2O + ferrocytochrome b-561
potassium ferrocyanide + H+ + ferricytochrome b-561
show the reaction diagram
-
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
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molybdenum cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Selenite
-
activates
[2Fe-2S]-center
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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+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.053 - 0.063
CO
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the portion of enzyme localized in the cytoplasm is low during exponential growth and high in stationary cells
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
3 * 14000 + 3 * 28000 + 3 * 85000
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
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2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
27000
-
deduced from sequence, Western blot
27800
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deduced from sequence, Western blot
28000
-
3 * 14000 + 3 * 28000 + 3 * 85000
30200
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
30700
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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
31500
-
deduced from sequence, Western blot
85000
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3 * 14000 + 3 * 28000 + 3 * 85000
87200
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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
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2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
140000
-
2 * 140000, SDS-PAGE
230000 - 300000
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230000
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sucrose density gradient centrifugation, sedimentation equilibrium experiments, gel filtration
280000 - 300000
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400000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
dimer
-
2 * 140000, SDS-PAGE
heterohexamer
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2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
hexamer
nonamer
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3 * 14000 + 3 * 28000 + 3 * 85000
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molybdoironflavoprotein
additional information
R384 has a gamma-hydroxy modification, C385 carries the catalytically essential S-selanyl-group
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
air-oxidized form
-
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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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genes for subunits L,M,S
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D38A
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similar to wild-type, mutation in the transmembrane domain
E177A
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similar to wild-type, mutation in the electron donating site
E196A
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23% activity, mutation in the electron donating site
F44A
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45% activity, mutation in the transmembrane domain
H105A
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similar to wild-type, mutation in the electron donating site
H112A
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similar to wild-type, mutation in the electron donating site
H117A
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inactive, residues involved in heme-binding
H156A
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inactive, residues involved in heme-binding
H47A
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inactive, residues involved in heme-binding
H83A
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inactive, residues involved in heme-binding
M51A
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similar to wild-type, mutation in the transmembrane domain
N106A
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similar to wild-type, mutation in the electron donating site
P48A
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similar to wild-type, mutation in the transmembrane domain
Q131A
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45% activity, mutation in the transmembrane domain
R149A
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25% activity, residue at the electron-accepting site of the protein
R67A
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incative, domain predicted to bind ascorbate at the electron-accepting site of the protein
S115A
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50% activity, mutation in the electron donating site
S118A
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similar to wild-type, mutation in the electron donating site
W119A
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17% activity, mutation in the electron donating site
Y190A
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similar to wild-type, mutation in the electron donating site
Y66A
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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)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)