The Enzyme Database

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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, (S)-mandelate dehydrogenase) [1,2]. The enzyme transfers the pro-R-hydrogen from NADH [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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]
[EC created 2014]
Accepted name: mandelamide amidase
Reaction: (R)-mandelamide + H2O = (R)-mandelate + NH3
Glossary: (R)-mandelate = (R)-2-hydroxy-2-phenylacetate
Other name(s): Pseudomonas mandelamide hydrolase
Systematic name: mandelamide hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Yamamoto, K., Oishi, K., Fujimatsu, I. and Komatsu, K. Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750. Appl. Environ. Microbiol. 57 (1991) 3028–3032. [PMID: 1660699]
[EC created 2000]
Accepted name: mandelate racemase
Reaction: (S)-mandelate = (R)-mandelate
Glossary: mandelate = 2-hydroxy-2-phenylacetate
Systematic name: mandelate racemase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9024-04-8
1.  Gunsalus, C.F., Stanier, R.Y. and Gunsalus, I.C. The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes. J. Bacteriol. 66 (1953) 548–553. [PMID: 13108854]
[EC created 1961]

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