(S)-mandelate dehydrogenase

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In enzymology, a (S)-mandelate dehydrogenase (EC 1.1.99.31) is an enzyme that catalyzes the chemical reaction

(S)-2-hydroxy-2-phenylacetate + acceptor $\rightleftharpoons$ 2-oxo-2-phenylacetate + reduced acceptor

Thus, the two substrates of this enzyme are (S)-2-hydroxy-2-phenylacetate and acceptor, whereas its two products are 2-oxo-2-phenylacetate and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (S)-2-hydroxy-2-phenylacetate:acceptor 2-oxidoreductase. This enzyme is also called MDH.

[edit] References

IUBMB entry for 1.1.99.31
BRENDA references for 1.1.99.31 (Recommended.)
PubMed references for 1.1.99.31
PubMed Central references for 1.1.99.31
Google Scholar references for 1.1.99.31
Lehoux IE, Mitra B (1999). "(S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects". Biochemistry. 38: 5836–48. doi:10.1021/bi990024m. PMID 10231535.
Dewanti AR, Xu Y, Mitra B (2004). "Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity". Biochemistry. 43: 10692–700. doi:10.1021/bi049005p. PMID 15311930.
Dewanti AR, Xu Y, Mitra B (2004). "Esters of mandelic acid as substrates for (S)-mandelate dehydrogenase from Pseudomonas putida: implications for the reaction mechanism". Biochemistry. 43: 1883–90. doi:10.1021/bi036021y. PMID 14967029.