The Enzyme Database

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Accepted name: D-arginine dehydrogenase
Reaction: D-arginine + acceptor + H2O = 5-guanidino-2-oxopentanoate + NH3 + reduced acceptor (overall reaction)
(1a) D-arginine + acceptor = iminoarginine + reduced acceptor
(1b) iminoarginine + H2O = 5-guanidino-2-oxopentanoate + NH3 (spontaneous)
Glossary: 5-guanidino-2-oxopentanoate = 2-ketoarginine
iminoarginine = 5-carbamimidamido-2-iminopentanoate
Other name(s): D-amino-acid:(acceptor) oxidoreductase (deaminating); D-amino-acid dehydrogenase; D-amino-acid:acceptor oxidoreductase (deaminating)
Systematic name: D-arginine:acceptor oxidoreductase (deaminating)
Comments: Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC, L-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine. The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. However, activity is maximal with D-arginine and D-lysine. Not active on glycine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37205-44-0
1.  Tsukada, K. D-Amino acid dehydrogenases of Pseudomonas fluorescens. J. Biol. Chem. 241 (1966) 4522–4528. [PMID: 5925166]
2.  Li, C. and Lu, C.D. Arginine racemization by coupled catabolic and anabolic dehydrogenases. Proc. Natl. Acad. Sci. USA 106 (2009) 906–911. [DOI] [PMID: 19139398]
3.  Fu, G., Yuan, H., Li, C., Lu, C.D., Gadda, G. and Weber, I.T. Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase. Biochemistry 49 (2010) 8535–8545. [DOI] [PMID: 20809650]
4.  Yuan, H., Fu, G., Brooks, P.T., Weber, I. and Gadda, G. Steady-state kinetic mechanism and reductive half-reaction of D-arginine dehydrogenase from Pseudomonas aeruginosa. Biochemistry 49 (2010) 9542–9550. [DOI] [PMID: 20932054]
5.  Fu, G., Yuan, H., Wang, S., Gadda, G. and Weber, I.T. Atomic-resolution structure of an N5 flavin adduct in D-arginine dehydrogenase. Biochemistry 50 (2011) 6292–6294. [DOI] [PMID: 21707047]
6.  Yuan, H., Xin, Y., Hamelberg, D. and Gadda, G. Insights on the mechanism of amine oxidation catalyzed by D-arginine dehydrogenase through pH and kinetic isotope effects. J. Am. Chem. Soc. 133 (2011) 18957–18965. [DOI] [PMID: 21999550]
[EC created 1972 as EC, transferred 2015 to EC, modified 2017]

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