KEGG   ENZYME: 1.1.99.31Help
Entry
EC 1.1.99.31                Enzyme                                 

Name
(S)-mandelate dehydrogenase;
MDH
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With other acceptors
BRITE hierarchy
Sysname
(S)-mandelate:acceptor 2-oxidoreductase
Reaction(IUBMB)
(S)-mandelate + acceptor = phenylglyoxylate + reduced acceptor [RN:R03793]
Reaction(KEGG)
R03793 > R07664;
(other) R04160
Show
Substrate
(S)-mandelate [CPD:C01984];
acceptor [CPD:C00028]
Product
phenylglyoxylate [CPD:C02137];
reduced acceptor [CPD:C00030]
Comment
This enzyme is a member of the FMN-dependent alpha-hydroxy-acid oxidase/dehydrogenase family [1]. While all enzymes of this family oxidize the (S)-enantiomer of an alpha-hydroxy acid to an alpha-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme. This enzyme transfers the electron pair from FMNH2 to a component of the electron transport chain, most probably ubiquinone [1,2]. It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy [2]. The enzyme has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate [1]. It also prefers substrates that, like (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3-yl)lactate [1]. Esters of mandelate, such as methyl (S)-mandelate, are also substrates [3].
History
EC 1.1.99.31 created 2006
Pathway
Aminobenzoate degradation
Microbial metabolism in diverse environments
Orthology
K15054  
(S)-mandelate dehydrogenase
Genes
PLU: 
SRR: 
SRL: 
SRY: 
SRS: 
SRA: 
SERR: 
PAO: 
RAH: 
RAQ: 
RAA: 
PPUN: 
PMK: 
PRE: 
MBS: 
CSA: 
HEL: 
HELO_1144(mdlB)
MMW: 
REU: 
REH: 
H16_B1832(mdlB)
CNC: 
BXE: 
BPH: 
BGL: 
BUG: 
BGE: 
BGF: 
BGD: 
BYI: 
BPX: 
PPK: 
PRB: 
BBR: 
BB1109(lldD)
BBM: 
BBH: 
AXO: 
AXN: 
PNA: 
ACK: 
VAP: 
VPD: 
HSE: 
AZO: 
azo2470(lldD)
AZA: 
TMZ: 
MCI: 
ARA: 
RTR: 
BJA: 
SNO: 
MSC: 
PDE: 
SWI: 
 » show all
Taxonomy
Reference
1  [PMID:10231535]
  Authors
Lehoux IE, Mitra B.
  Title
(S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects.
  Journal
Biochemistry. 38 (1999) 5836-48.
  Organism
Pseudomonas putida
Reference
2  [PMID:15311930]
  Authors
Dewanti AR, Xu Y, Mitra B.
  Title
Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity.
  Journal
Biochemistry. 43 (2004) 10692-700.
  Organism
Pseudomonas putida
Reference
3  [PMID:14967029]
  Authors
Dewanti AR, Xu Y, Mitra B.
  Title
Esters of mandelic acid as substrates for (S)-mandelate dehydrogenase from Pseudomonas putida: implications for the reaction mechanism.
  Journal
Biochemistry. 43 (2004) 1883-90.
  Organism
Pseudomonas putida
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
9067-95-2

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