| EC |
1.1.99.30 |
| Accepted name: |
2-oxo-acid reductase |
| Reaction: |
a (2R)-hydroxy-carboxylate + acceptor = a 2-oxocarboxylate + reduced acceptor |
| Other name(s): |
(2R)-hydroxycarboxylate-viologen-oxidoreductase; HVOR; 2-oxoacid reductase |
| Systematic name: |
(2R)-hydroxy-carboxylate:acceptor oxidoreductase |
| Comments: |
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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115299-99-5 |
| References: |
| 1. |
Trautwein, T., Krauss, F., Lottspeich, F. and Simon, H. The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. Eur. J. Biochem. 222 (1994) 1025–1032. [DOI] [PMID: 8026480] |
| 2. |
Neumann, S. and Simon, H. On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad specificity from two Proteus species. FEBS Lett. 167 (1985) 29–32. |
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| [EC 1.1.99.30 created 2004] |
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