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

EC NUMBER
COMMENTARY hide
1.2.2.4
-
RECOMMENDED NAME
GeneOntology No.
carbon-monoxide dehydrogenase (cytochrome b-561)
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
64972-88-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
-
-
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
-
molybdenum cofactor
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+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.053 - 0.063
CO
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
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
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
27000
-
deduced from sequence, Western blot
27800
-
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
-
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
-
3 * 14000 + 3 * 28000 + 3 * 85000
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
140000
-
2 * 140000, SDS-PAGE
230000 - 300000
-
-
230000
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sucrose density gradient centrifugation, sedimentation equilibrium experiments, gel filtration
280000 - 300000
-
-
400000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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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
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
-
3 * 14000 + 3 * 28000 + 3 * 85000
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molybdoironflavoprotein
additional information
R384 has a gamma-hydroxy modification, C385 carries the catalytically essential S-selanyl-group
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
air-oxidized form
-
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
-
inactive, residues involved in heme-binding
H83A
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inactive, residues involved in heme-binding
M51A
-
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
-
similar to wild-type, mutation in the transmembrane domain
Q131A
-
45% activity, mutation in the transmembrane domain
R149A
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25% activity, residue at the electron-accepting site of the protein
R67A
-
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
-
similar to wild-type, mutation in the electron donating site
Y66A
-
incative, domain predicted to bind ascorbate at the electron-accepting site of the protein