D-amino acid dehydrogenase

D-amino-acid dehydrogenase (EC 1.4.99.1) 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.^[1] The enzyme has a very broad specificity and can act on most D-amino acids.^[2]

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.^[1][3]

See also

• Oxidative phosphorylation
• Electron transport chain
• Microbial metabolism

References

1. ^ ^{a b} 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. http://www.jbc.org/cgi/reprint/255/10/4487. 
2. ^ Tsukada K (10 October 1966). "D-amino acid dehydrogenases of Pseudomonas fluorescens". J. Biol. Chem. 241 (19): 4522–8. PMID 5925166. http://www.jbc.org/cgi/reprint/241/19/4522. 
3. ^ 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. 

External links

• BRENDA entry on EC 1.4.99.1
• ENZYME entry on EC 1.4.99.1

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