D-amino acid dehydrogenase
Overview
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
References
- ↑ 1.0 1.1 Olsiewski PJ, Kaczorowski GJ, Walsh C (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 (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. PMID 6131836.
External links
CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases | |
|---|---|
| 1.4.1 - NAD/NADP acceptor | Glutamate dehydrogenase (GLUD1) |
| 1.4.3 - oxygen acceptor | D-amino acid oxidase - Amine oxidase - Lysyl oxidase - Monoamine oxidase |
| 1.4.4 - disulfide acceptor | Glycine decarboxylase complex |
| 1.4.99 - other acceptors | D-amino acid dehydrogenase - Amine dehydrogenase |
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