BRENDA - Enzyme Database
show all sequences of 1.2.5.3

Kinetic and spectroscopic studies of the molybdenum-copper CO dehydrogenase from Oligotropha carboxidovorans

Zhang, B.; Hemann, C.F.; Hille, R.; J. Biol. Chem. 285, 12571-12578 (2010)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
rapid reaction kinetics, steady-state kinetics
Oligotropha carboxidovorans
0.0107
-
CO
pH 7.2, 25°C
Oligotropha carboxidovorans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Cu
essential for enzyme activity, 1.69 Cu per mol of enzyme dimer
Oligotropha carboxidovorans
Fe2+
8.05 Fe per mol of enzyme dimer, in the Fe-S cluster
Oligotropha carboxidovorans
Mo3+
essential for enzyme activity, 1.82 Mo per mol of enzyme dimer
Oligotropha carboxidovorans
additional information
metal contents are determined by inductively coupled plasma atomic emission spectrometry
Oligotropha carboxidovorans
Se
-
Oligotropha carboxidovorans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
CO + a quinone + H2O
Oligotropha carboxidovorans
-
CO2 + a quinol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oligotropha carboxidovorans
-
-
-
Reaction
Reaction
Commentary
Organism
CO + a quinone + H2O = CO2 + a quinol
CO initially binds rapidly to the enzyme, possibly at the Cu(I) of the active site, prior to undergoing oxidation. A Mo(V) species exhibits strong coupling to the copper of the active center, the rate-limiting step of overall turnover is likely in the reductive half-reaction
Oligotropha carboxidovorans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CO + a quinone + H2O
-
725392
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
CO + a quinone + H2O
the enzyme catalyzes the oxidation of CO to CO2, yielding two electrons and two H+
725392
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Oligotropha carboxidovorans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
51.1
-
CO
pH 7.2, 25°C, reductive half-reaction of enzyme CODH with CO
Oligotropha carboxidovorans
93.3
-
CO
pH 7.2, 25°C
Oligotropha carboxidovorans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
-
Oligotropha carboxidovorans
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
10
only modest loss of activity at these extreme pHs indicates that ionization of functional groups in the active site is not as critical to catalysis for CODH
Oligotropha carboxidovorans
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Oligotropha carboxidovorans
additional information
presence of FAD, Fe/S clusters, and a [CuSMoO2] coordination in the active site determined by Raman spectra
Oligotropha carboxidovorans
[CuSMoO2] cofactor
-
Oligotropha carboxidovorans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Oligotropha carboxidovorans
additional information
presence of FAD, Fe/S clusters, and a [CuSMoO2] coordination in the active site determined by Raman spectra
Oligotropha carboxidovorans
[CuSMoO2] cofactor
-
Oligotropha carboxidovorans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
rapid reaction kinetics, steady-state kinetics
Oligotropha carboxidovorans
0.0107
-
CO
pH 7.2, 25°C
Oligotropha carboxidovorans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Cu
essential for enzyme activity, 1.69 Cu per mol of enzyme dimer
Oligotropha carboxidovorans
Fe2+
8.05 Fe per mol of enzyme dimer, in the Fe-S cluster
Oligotropha carboxidovorans
Mo3+
essential for enzyme activity, 1.82 Mo per mol of enzyme dimer
Oligotropha carboxidovorans
additional information
metal contents are determined by inductively coupled plasma atomic emission spectrometry
Oligotropha carboxidovorans
Se
-
Oligotropha carboxidovorans
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
Oligotropha carboxidovorans
-
CO2 + a quinol
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CO + a quinone + H2O
-
725392
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
CO + a quinone + H2O
the enzyme catalyzes the oxidation of CO to CO2, yielding two electrons and two H+
725392
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Oligotropha carboxidovorans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
51.1
-
CO
pH 7.2, 25°C, reductive half-reaction of enzyme CODH with CO
Oligotropha carboxidovorans
93.3
-
CO
pH 7.2, 25°C
Oligotropha carboxidovorans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
-
Oligotropha carboxidovorans
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
10
only modest loss of activity at these extreme pHs indicates that ionization of functional groups in the active site is not as critical to catalysis for CODH
Oligotropha carboxidovorans
General Information
General Information
Commentary
Organism
physiological function
Oligotropha carboxidovorans is a carboxydotrophic bacterium capable of aerobic, chemolithoautotrophic growth using COas a sole source of carbon and energy. The key enzyme involved in this facultative metabolism is an air-stable molybdenum-containing CO dehydrogenase that catalyzes the oxidation of CO to CO2
Oligotropha carboxidovorans
General Information (protein specific)
General Information
Commentary
Organism
physiological function
Oligotropha carboxidovorans is a carboxydotrophic bacterium capable of aerobic, chemolithoautotrophic growth using COas a sole source of carbon and energy. The key enzyme involved in this facultative metabolism is an air-stable molybdenum-containing CO dehydrogenase that catalyzes the oxidation of CO to CO2
Oligotropha carboxidovorans
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
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1
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4
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735935
Stein
Orbital contributions to CO ox ...
Hydrogenophaga pseudoflava, Oligotropha carboxidovorans
Chem. Commun. (Camb.)
50
1104-1106
2014
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2
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4
4
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736513
Pelzmann
Insights into the posttranslat ...
Oligotropha carboxidovorans
J. Biol. Inorg. Chem.
19
1399-1414
2014
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1
4
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1
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1
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1
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1
1
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4
4
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736437
Wilcoxen
The hydrogenase activity of th ...
Oligotropha carboxidovorans
J. Biol. Chem.
288
36052-36060
2013
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4
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1
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1
1
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1
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4
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1
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3
1
1
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1
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1
1
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725197
Wilcoxen
Substitution of silver for cop ...
Oligotropha carboxidovorans
J. Am. Chem. Soc.
133
12934-12936
2011
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1
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1
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2
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3
3
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735667
Wilcoxen
Reaction of the molybdenum- an ...
, Oligotropha carboxidovorans ATCC 49405
Biochemistry
50
1910-1916
2011
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1
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11
1
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2
2
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725052
Nishimura
-
Purification and characterizat ...
Aeropyrum pernix, Aeropyrum pernix TB5
Fish. Sci.
76
999-1006
2010
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1
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1
4
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6
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4
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8
2
1
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1
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2
2
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725392
Zhang
Kinetic and spectroscopic stud ...
Oligotropha carboxidovorans
J. Biol. Chem.
285
12571-12578
2010
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1
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1
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1
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5
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1
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1
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1
1
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1
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736301
Gourlay
Paramagnetic active site model ...
Oligotropha carboxidovorans
J. Am. Chem. Soc.
128
2164-2165
2006
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2
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736512
Resch
Structural and functional reco ...
Oligotropha carboxidovorans, Oligotropha carboxidovorans DSM 1227
J. Biol. Inorg. Chem.
10
518-528
2005
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1
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390484
Lorite
Carbon monoxide dehydrogenase ...
Bradyrhizobium japonicum, Bradyrhizobium japonicum 110spc4
Appl. Environ. Microbiol.
66
1871-1876
2000
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656481
Hanzelmann
The effect of intracellular mo ...
Hydrogenophaga pseudoflava, Hydrogenophaga pseudoflava DSM 1084
J. Mol. Biol.
301
1221-1235
2000
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736397
Gremer
Binding of flavin adenine dinu ...
Oligotropha carboxidovorans, Oligotropha carboxidovorans DSM 1227
J. Biol. Chem.
275
1864-1872
2000
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390482
Dobbek
Crystal structure and mechanis ...
Oligotropha carboxidovorans
Proc. Natl. Acad. Sci. USA
96
8884-8889
1999
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390483
Kang
Cloning and molecular characte ...
Hydrogenophaga pseudoflava, Hydrogenophaga pseudoflava DSM 1084
J. Bacteriol.
181
5581-5590
1999
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390479
Schubel
Molecular characterization of ...
Oligotropha carboxidovorans, Oligotropha carboxidovorans OM5
J. Bacteriol.
177
2197-2203
1995
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