BRENDA - Enzyme Database
show all sequences of 1.2.5.3

Reaction of the molybdenum- and copper-containing carbon monoxide dehydrogenase from Oligotropha carboxydovorans with quinones

Wilcoxen, J.; Zhang, B.; Hille, R.; Biochemistry 50, 1910-1916 (2011)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
CO + a quinone + H2O
-
-
CO2 + a quinol
-
-
?
CO + a quinone + H2O
Oligotropha carboxidovorans ATCC 49405
-
CO2 + a quinol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oligotropha carboxidovorans ATCC 49405
P19919 AND P19920 AND P19921
genes coxL, coxM, and coxS; genes coxS, coxM, and coxL
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
-
735667
-
CO2 + 1,2-naphthoquinol-4-sulfonic acid
-
-
-
?
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
-
735667
Oligotropha carboxidovorans ATCC 49405
CO2 + 1,2-naphthoquinol-4-sulfonic acid
-
-
-
?
CO + 1,4-naphthoquinone + H2O
-
735667
-
CO2 + 1,4-naphthoquinol
-
-
-
?
CO + 1,4-naphthoquinone + H2O
-
735667
Oligotropha carboxidovorans ATCC 49405
CO2 + 1,4-naphthoquinol
-
-
-
?
CO + a quinone + H2O
-
735667
-
CO2 + a quinol
-
-
-
?
CO + a quinone + H2O
-
735667
Oligotropha carboxidovorans ATCC 49405
CO2 + a quinol
-
-
-
?
CO + benzoquinone + H2O
-
735667
-
CO2 + benzoquinol
-
-
-
?
CO + benzoquinone + H2O
-
735667
Oligotropha carboxidovorans ATCC 49405
CO2 + benzoquinol
-
-
-
?
CO + ubiquinone-1 + H2O
-
735667
-
CO2 + ubiquinol-1
-
-
-
?
additional information
routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site
735667
-
?
-
-
-
-
additional information
routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site
735667
Oligotropha carboxidovorans ATCC 49405
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
heterohexamer
the functional enzyme is a (alphabetagamma)2 hexamer that consists of a small 17.8 kDa subunit (CoxS) containing two [2Fe-2S] clusters, a medium 30.2 kDa subunit (CoxM) containing an FAD cofactor, and a large 88.7 kDa subunit (CoxL) that possesses the molybdenum center
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
CO + a quinone + H2O
-
-
CO2 + a quinol
-
-
?
CO + a quinone + H2O
Oligotropha carboxidovorans ATCC 49405
-
CO2 + a quinol
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
-
735667
-
CO2 + 1,2-naphthoquinol-4-sulfonic acid
-
-
-
?
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
-
735667
Oligotropha carboxidovorans ATCC 49405
CO2 + 1,2-naphthoquinol-4-sulfonic acid
-
-
-
?
CO + 1,4-naphthoquinone + H2O
-
735667
-
CO2 + 1,4-naphthoquinol
-
-
-
?
CO + 1,4-naphthoquinone + H2O
-
735667
Oligotropha carboxidovorans ATCC 49405
CO2 + 1,4-naphthoquinol
-
-
-
?
CO + a quinone + H2O
-
735667
-
CO2 + a quinol
-
-
-
?
CO + a quinone + H2O
-
735667
Oligotropha carboxidovorans ATCC 49405
CO2 + a quinol
-
-
-
?
CO + benzoquinone + H2O
-
735667
-
CO2 + benzoquinol
-
-
-
?
CO + benzoquinone + H2O
-
735667
Oligotropha carboxidovorans ATCC 49405
CO2 + benzoquinol
-
-
-
?
CO + ubiquinone-1 + H2O
-
735667
-
CO2 + ubiquinol-1
-
-
-
?
additional information
routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site
735667
-
?
-
-
-
-
additional information
routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site
735667
Oligotropha carboxidovorans ATCC 49405
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
heterohexamer
the functional enzyme is a (alphabetagamma)2 hexamer that consists of a small 17.8 kDa subunit (CoxS) containing two [2Fe-2S] clusters, a medium 30.2 kDa subunit (CoxM) containing an FAD cofactor, and a large 88.7 kDa subunit (CoxL) that possesses the molybdenum center
-
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the XOR family
-
physiological function
carbon monoxide dehydrogenase from Oligotropha carboxydovorans catalyzes the oxidation of carbon monoxide to carbon dioxide, providing the organism both a carbon source and energy for growth. In the oxidative half of the catalytic cycle, electrons gained from CO are ultimately passed to the electron transport chain of the Gram-negative organism. Quinones are catalytically competent as proximal acceptor of reducing equivalents from the enzyme
-
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the XOR family
-
physiological function
carbon monoxide dehydrogenase from Oligotropha carboxydovorans catalyzes the oxidation of carbon monoxide to carbon dioxide, providing the organism both a carbon source and energy for growth. In the oxidative half of the catalytic cycle, electrons gained from CO are ultimately passed to the electron transport chain of the Gram-negative organism. Quinones are catalytically competent as proximal acceptor of reducing equivalents from the enzyme
-
Other publictions for EC 1.2.5.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736514
Hille
The aerobic CO dehydrogenase f ...
Oligotropha carboxidovorans
J. Biol. Inorg. Chem.
20
243-251
2015
-
-
1
1
-
-
2
-
1
3
-
2
-
2
-
-
-
1
-
-
-
-
6
1
-
-
-
-
-
-
-
5
-
-
-
-
-
1
5
1
-
-
-
2
-
-
1
3
-
2
-
-
-
-
-
-
-
-
6
1
-
-
-
-
-
-
-
-
-
4
4
-
-
-
735935
Stein
Orbital contributions to CO ox ...
Hydrogenophaga pseudoflava, Oligotropha carboxidovorans
Chem. Commun. (Camb.)
50
1104-1106
2014
-
-
-
-
-
-
2
-
-
4
-
2
-
2
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
4
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
4
4
-
-
-
736513
Pelzmann
Insights into the posttranslat ...
Oligotropha carboxidovorans
J. Biol. Inorg. Chem.
19
1399-1414
2014
-
-
-
-
1
-
-
-
1
4
-
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
1
-
-
-
-
-
1
4
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
4
4
-
-
-
736437
Wilcoxen
The hydrogenase activity of th ...
Oligotropha carboxidovorans
J. Biol. Chem.
288
36052-36060
2013
-
-
-
-
-
-
-
-
-
4
-
1
-
2
-
-
-
-
-
-
-
-
3
1
1
-
-
-
1
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
-
-
3
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
725197
Wilcoxen
Substitution of silver for cop ...
Oligotropha carboxidovorans
J. Am. Chem. Soc.
133
12934-12936
2011
-
-
1
1
-
-
-
-
-
2
2
1
-
1
-
-
-
-
-
1
-
-
2
2
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
-
-
-
-
2
2
1
-
-
-
-
-
1
-
-
2
2
-
-
-
-
-
-
-
-
-
3
3
-
-
-
735667
Wilcoxen
Reaction of the molybdenum- an ...
, Oligotropha carboxidovorans ATCC 49405
Biochemistry
50
1910-1916
2011
-
-
-
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
11
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
11
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
725052
Nishimura
-
Purification and characterizat ...
Aeropyrum pernix, Aeropyrum pernix TB5
Fish. Sci.
76
999-1006
2010
-
-
1
-
-
-
-
-
-
1
4
-
-
2
-
-
1
-
-
-
4
-
8
2
1
-
2
-
1
-
-
6
-
-
-
-
-
1
6
-
-
-
-
-
-
-
-
1
4
-
-
-
-
1
-
-
4
-
8
2
1
-
2
-
1
-
-
-
-
2
2
-
-
-
725392
Zhang
Kinetic and spectroscopic stud ...
Oligotropha carboxidovorans
J. Biol. Chem.
285
12571-12578
2010
-
-
-
-
-
-
-
2
-
5
-
1
-
3
-
-
-
1
-
-
-
-
2
-
1
-
-
2
1
1
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
2
-
5
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
2
1
1
-
-
-
1
1
-
-
-
736301
Gourlay
Paramagnetic active site model ...
Oligotropha carboxidovorans
J. Am. Chem. Soc.
128
2164-2165
2006
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
736512
Resch
Structural and functional reco ...
Oligotropha carboxidovorans, Oligotropha carboxidovorans DSM 1227
J. Biol. Inorg. Chem.
10
518-528
2005
-
-
-
1
-
-
-
-
-
6
-
-
-
3
-
-
-
-
1
-
-
-
2
1
1
-
-
-
1
-
-
2
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
6
-
-
-
-
-
-
1
-
-
-
2
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
390484
Lorite
Carbon monoxide dehydrogenase ...
Bradyrhizobium japonicum, Bradyrhizobium japonicum 110spc4
Appl. Environ. Microbiol.
66
1871-1876
2000
-
-
-
-
-
-
1
-
1
3
4
-
-
2
-
-
1
-
-
1
1
-
-
1
1
-
-
-
1
-
-
4
-
-
-
-
-
-
4
-
-
-
-
1
-
-
1
3
4
-
-
-
-
1
-
1
1
-
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
656481
Hanzelmann
The effect of intracellular mo ...
Hydrogenophaga pseudoflava, Hydrogenophaga pseudoflava DSM 1084
J. Mol. Biol.
301
1221-1235
2000
-
-
-
1
-
-
-
-
-
5
-
2
-
2
-
1
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
1
-
-
-
-
-
-
-
5
-
2
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
736397
Gremer
Binding of flavin adenine dinu ...
Oligotropha carboxidovorans, Oligotropha carboxidovorans DSM 1227
J. Biol. Chem.
275
1864-1872
2000
-
-
1
-
1
-
-
-
-
4
4
-
-
6
-
-
1
-
-
-
-
-
-
2
1
-
-
-
1
-
-
3
-
-
-
-
-
1
3
-
1
-
-
-
-
-
-
4
4
-
-
-
-
1
-
-
-
-
-
2
1
-
-
-
1
-
-
-
-
2
2
-
-
-
390482
Dobbek
Crystal structure and mechanis ...
Oligotropha carboxidovorans
Proc. Natl. Acad. Sci. USA
96
8884-8889
1999
-
-
-
1
-
-
-
-
-
4
-
-
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
1
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
390483
Kang
Cloning and molecular characte ...
Hydrogenophaga pseudoflava, Hydrogenophaga pseudoflava DSM 1084
J. Bacteriol.
181
5581-5590
1999
-
-
1
-
-
-
-
-
-
3
3
-
-
2
-
-
1
-
-
-
-
-
2
1
1
-
-
-
1
-
-
2
-
3
-
-
-
1
2
-
-
-
-
-
-
-
-
3
3
-
-
-
-
1
-
-
-
-
2
1
1
-
-
-
1
-
-
3
-
1
1
-
-
-
390479
Schubel
Molecular characterization of ...
Oligotropha carboxidovorans, Oligotropha carboxidovorans OM5
J. Bacteriol.
177
2197-2203
1995
-
-
1
-
-
-
-
-
-
2
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-