KEGG   ENZYME: 1.1.1.379
Entry
EC 1.1.1.379                Enzyme                                 

Name
(R)-mandelate dehydrogenase;
ManDH2;
D-ManDH2;
D-mandelate dehydrogenase (ambiguous)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
(R)-mandelate:NAD+ 2-oxidoreductase
Reaction(IUBMB)
(R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+ [RN:R03790]
Reaction(KEGG)
R03790
Substrate
(R)-mandelate [CPD:C01983];
NAD+ [CPD:C00003]
Product
phenylglyoxylate [CPD:C02137];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
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].
History
EC 1.1.1.379 created 2014
Reference
1
  Authors
Baker, D.P. and Fewson, C.A.
  Title
Purification and characterization of D(-)-mandelate dehydrogenase from Rhodotorula graminis.
  Journal
Microbiology 135:2035-2044 (1989)
Reference
2  [PMID:1731758]
  Authors
Baker DP, Kleanthous C, Keen JN, Weinhold E, Fewson CA
  Title
Mechanistic and active-site studies on D(--)-mandelate dehydrogenase from Rhodotorula graminis.
  Journal
Biochem J 281 ( Pt 1):211-8 (1992)
DOI:10.1042/bj2810211
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.379
IUBMB Enzyme Nomenclature: 1.1.1.379
ExPASy - ENZYME nomenclature database: 1.1.1.379
BRENDA, the Enzyme Database: 1.1.1.379

  All links  
Chemical substance (5)   
   KEGG COMPOUND (5)   
Chemical reaction (2)   
   KEGG REACTION (1)   
   KEGG RCLASS (1)   
All databases (7)   

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