| EC |
1.1.1.379 |
| Accepted name: |
(R)-mandelate dehydrogenase |
| Reaction: |
(R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+ |
| Glossary: |
(R)-mandelate = D-mandelate |
| Other name(s): |
ManDH2; D-ManDH2; D-mandelate dehydrogenase (ambiguous) |
| Systematic name: |
(R)-mandelate:NAD+ 2-oxidoreductase |
| Comments: |
The enzyme, found in bacteria and fungi, can also accept a number of substituted mandelate derivatives, such as 3-hydroxymandelate, 4-hydroxymandelate, 2-methoxymandelate, 4-hydroxy-3-methoxymandelate and 3-hydroxy-4-methoxymandelate. The enzyme has no activity with (S)-mandelate (cf. EC 1.1.99.31, (S)-mandelate dehydrogenase) [1,2]. The enzyme transfers the pro-R-hydrogen from NADH [2]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Baker, D.P. and Fewson, C.A. Purification and characterization of D(–)-mandelate dehydrogenase from Rhodotorula graminis. Microbiology 135 (1989) 2035–2044. |
| 2. |
Baker, D.P., Kleanthous, C., Keen, J.N., Weinhold, E. and Fewson, C.A. Mechanistic and active-site studies on D(–)-mandelate dehydrogenase from Rhodotorula graminis. Biochem. J. 281 (1992) 211–218. [PMID: 1731758] |
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| [EC 1.1.1.379 created 2014] |
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