D-amino acid dehydrogenase
D-amino-acid dehydrogenase (EC 184.108.40.206) is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids.
D-amino acid + H2O + acceptor <=> a 2-oxo acid + NH3 + reduced acceptor
This reaction is distinct from the oxidation reaction catalysed by D-amino acid oxidase that uses oxygen as a second substrate, as the dehydrogenase can use many different compounds as electron acceptors, with the physiological substrate being coenzyme Q.
- Olsiewski PJ, Kaczorowski GJ, Walsh C (25 May 1980). "Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B". J. Biol. Chem. 255 (10): 4487–94. PMID 6102989.
- Tsukada K (10 October 1966). "D-amino acid dehydrogenases of Pseudomonas fluorescens". J. Biol. Chem. 241 (19): 4522–8. PMID 5925166.
- Jones H, Venables WA (1983). "Effects of solubilisation on some properties of the membrane-bound respiratory enzyme D-amino acid dehydrogenase of Escherichia coli". FEBS Lett. 151 (2): 189–92. doi:10.1016/0014-5793(83)80066-0. PMID 6131836.
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