BRENDA - Enzyme Database
show all sequences of 1.2.5.3

Substitution of silver for copper in the binuclear Mo/Cu center of carbon monoxide dehydrogenase from Oligotropha carboxidovorans

Wilcoxen, J.; Snider, S.; Hille, R.; J. Am. Chem. Soc. 133, 12934-12936 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
the enzyme is encoded by the megaplasmid-localized coxBCMSLDEFGHIK gene cluster, the cosMSL structural genes encoding the enzyme
Oligotropha carboxidovorans
Crystallization (Commentary)
Crystallization
Organism
crystal structure analysis
Oligotropha carboxidovorans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
the small subunit CoxS harbors two [2Fe-2S] iron-sulfur clusters
Oligotropha carboxidovorans
Molybdenum
-
Oligotropha carboxidovorans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
(alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE
Oligotropha carboxidovorans
89000
-
(alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE
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
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
additional information
Oligotropha carboxidovorans is aerobe and able to grow with CO as sole source of both carbon and energy
Oligotropha carboxidovorans
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CO + a quinone + H2O
-
725197
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
additional information
quinones are unusual physiological oxidants for this family of enzymes
725197
Oligotropha carboxidovorans
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
heterohexamer
(alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE
Oligotropha carboxidovorans
More
the the active site molybdenum center is located in the large subunit, while the medium subunit contains FAD, and the small subunit contains the [2Fe-2S]-clusters
Oligotropha carboxidovorans
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
bound by the medium subunit
Oligotropha carboxidovorans
molybdenum-containing cofactor
the active site molybdenum center located in teh large subunit. The molybdenum becomes reduced in the final step of the reaction
Oligotropha carboxidovorans
Cloned(Commentary) (protein specific)
Commentary
Organism
the enzyme is encoded by the megaplasmid-localized coxBCMSLDEFGHIK gene cluster, the cosMSL structural genes encoding the enzyme
Oligotropha carboxidovorans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
bound by the medium subunit
Oligotropha carboxidovorans
molybdenum-containing cofactor
the active site molybdenum center located in teh large subunit. The molybdenum becomes reduced in the final step of the reaction
Oligotropha carboxidovorans
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure analysis
Oligotropha carboxidovorans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
the small subunit CoxS harbors two [2Fe-2S] iron-sulfur clusters
Oligotropha carboxidovorans
Molybdenum
-
Oligotropha carboxidovorans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
(alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE
Oligotropha carboxidovorans
89000
-
(alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE
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
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
additional information
Oligotropha carboxidovorans is aerobe and able to grow with CO as sole source of both carbon and energy
Oligotropha carboxidovorans
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CO + a quinone + H2O
-
725197
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
additional information
quinones are unusual physiological oxidants for this family of enzymes
725197
Oligotropha carboxidovorans
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
heterohexamer
(alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE
Oligotropha carboxidovorans
More
the the active site molybdenum center is located in the large subunit, while the medium subunit contains FAD, and the small subunit contains the [2Fe-2S]-clusters
Oligotropha carboxidovorans
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the noncanonical members of the xanthine oxidase family. The Mo-containing CO dehydrogenase from Oligotropha carboxidovorans and related organisms is distinct from the highly O2-sensitive Ni/Fe-containing CO dehydrogenase from obligate anaerobes such as Clostridum thermoaceticum or Methanosarcina barkerii. Quinones are unusual physiological oxidants for this family of enzymes, the overall fold of the FAD-containing domain of CO dehydrogenase resembles the dehydrogenase rather than the oxidase form of the bovine xanthine oxidoreductase, particularly with regard to the position of the mobile loop referred to above that is involved in the Dto-O conversion, but there are significant differences in the environment of the FAD in CO dehydrogenase and xanthine dehydrogenase. A Lys-Asp pair near the pyrimidine subnucleus of the flavin is preserved, for example, but the positions of the Ile and aromatic residues are reversed, with the Ile on the re side and Tyr (a Phe in the bovine enzyme) on the si side of the isoalloxazine ring
Oligotropha carboxidovorans
metabolism
the enzyme catalyzes the critical first step in this process, the oxidation of CO to CO2 with the reducing equivalents thus obtained ultimately being passed on ultimately to a CO-insensitive terminal oxidase
Oligotropha carboxidovorans
additional information
the enzyme is noncanonical in terms of the structure of the molybdenum center, the nature of the reaction catalyzed, the type of redox-active centers that are found, or some combination of these. The active site is located in the large subunit
Oligotropha carboxidovorans
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the noncanonical members of the xanthine oxidase family. The Mo-containing CO dehydrogenase from Oligotropha carboxidovorans and related organisms is distinct from the highly O2-sensitive Ni/Fe-containing CO dehydrogenase from obligate anaerobes such as Clostridum thermoaceticum or Methanosarcina barkerii. Quinones are unusual physiological oxidants for this family of enzymes, the overall fold of the FAD-containing domain of CO dehydrogenase resembles the dehydrogenase rather than the oxidase form of the bovine xanthine oxidoreductase, particularly with regard to the position of the mobile loop referred to above that is involved in the Dto-O conversion, but there are significant differences in the environment of the FAD in CO dehydrogenase and xanthine dehydrogenase. A Lys-Asp pair near the pyrimidine subnucleus of the flavin is preserved, for example, but the positions of the Ile and aromatic residues are reversed, with the Ile on the re side and Tyr (a Phe in the bovine enzyme) on the si side of the isoalloxazine ring
Oligotropha carboxidovorans
metabolism
the enzyme catalyzes the critical first step in this process, the oxidation of CO to CO2 with the reducing equivalents thus obtained ultimately being passed on ultimately to a CO-insensitive terminal oxidase
Oligotropha carboxidovorans
additional information
the enzyme is noncanonical in terms of the structure of the molybdenum center, the nature of the reaction catalyzed, the type of redox-active centers that are found, or some combination of these. The active site is located in the large subunit
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
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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4
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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
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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725197
Wilcoxen
Substitution of silver for cop ...
Oligotropha carboxidovorans
J. Am. Chem. Soc.
133
12934-12936
2011
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1
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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2
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3
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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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8
2
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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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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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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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