(S)-mandelate dehydrogenase

Class of enzymes (S)-mandelate dehydrogenase 1.1.99.31 In enzymology, (S)-mandelate dehydrogenase (1.1.99.31) (MDH), is an enzyme that catalyzes the chemical reaction. alt=|frameless + acceptor = frameless + reduced acceptor (S)-Mandelate 2-oxo-2-phenylacetate (S)-2-hydroxy-2-phenylacetate + acceptor ⇌ 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 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. The enzyme has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate. It also prefers substrates that, like (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3-yl)lactate. Esters of mandelate, such as methyl (S)-mandelate, are also substrates.Information on EC 1.1.99.31 - (S)-mandelate dehydrogenase https://www.brenda-enzymes.org/enzyme.php?ecno=1.1.99.31 live https://web.archive.org/web/20150908192707/http://www.brenda-enzymes.org/enzyme.php?ecno=1.1.99.31 2015-09-08 Synonyms (S)-mandelate dehydrogenase is also knows as: L-mandelate dehydrogenase, L-MDH, MDH, SManDH, and SMDH. References 30em 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 10231535 10.1021/bi990024m 18 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 15311930 10.1021/bi049005p 33 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 14967029 10.1021/bi036021y 7 Biology no Category:EC 1.1.99 Category:Enzymes of unknown structure