| Entry |
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| Name |
2-oxo-acid reductase;
(2R)-hydroxycarboxylate-viologen-oxidoreductase;
HVOR;
2-oxoacid reductase
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| Class |
Oxidoreductases;
Acting on the CH-OH group of donors;
With other acceptors
 |
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| Sysname |
(2R)-hydroxy-carboxylate:acceptor oxidoreductase
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| Reaction(IUBMB) |
a (2R)-hydroxy-carboxylate + acceptor = a 2-oxo-carboxylate + reduced acceptor [RN: R07155]
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| Reaction(KEGG) |
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| Substrate |
(2R)-hydroxy-carboxylate [CPD: C15487];
acceptor [CPD: C00028]
|
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| Product |
2-oxo-carboxylate;
reduced acceptor [CPD: C00030]
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| Comment |
Contains [4Fe-4S] and a mononucleotide molybdenum (pyranopterin) cofactor. Has broad substrate specificity, with 2-oxo-monocarboxylates and 2-oxo-dicarboxylates acting as substrates. Branching in a substrate at the C-3 position results in loss of activity. The enzyme from Proteus sp. is inactivated by oxygen.
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| Reference |
|
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| Authors |
Trautwein T, Krauss F, Lottspeich F, Simon H. |
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| Title |
The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. |
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| Journal |
Eur. J. Biochem. 222 (1994) 1025-32. |
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| Organism |
Proteus vulgaris |
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| Reference |
2 |
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| Authors |
Neumann, S. and Simon, H. |
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| Title |
On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad specificity from two Proteus species. |
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| Journal |
FEBS Lett. 167 (1985) 29-32. |
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| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 115299-99-5 |
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