EC - D-arginine dehydrogenase

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IntEnz Enzyme Nomenclature


Accepted name:
D-arginine dehydrogenase
Other names:
D-amino-acid:(acceptor) oxidoreductase (deaminating)
D-amino-acid dehydrogenase
D-amino-acid:acceptor oxidoreductase (deaminating)
Systematic name:
D-arginine:acceptor oxidoreductase (deaminating)




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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Tsukada, K.
    D-Amino acid dehydrogenases of Pseudomonas fluorescens.
    J. Biol. Chem. 241 : 4522-4528 (1966). [PMID: 5925166]
  2. Li, C., Lu, C. D.
    Arginine racemization by coupled catabolic and anabolic dehydrogenases.
    Proc. Natl. Acad. Sci. U.S.A. 106 : 906-911 (2009). [PMID: 19139398]
  3. Fu, G., Yuan, H., Li, C., Lu, C. D., Gadda, G., Weber, I. T.
    Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase.
    Biochemistry 49 : 8535-8545 (2010). [PMID: 20809650]
  4. Yuan, H., Fu, G., Brooks, P. T., Weber, I., Gadda, G.
    Steady-state kinetic mechanism and reductive half-reaction of D-arginine dehydrogenase from Pseudomonas aeruginosa.
    Biochemistry 49 : 9542-9550 (2010). [PMID: 20932054]
  5. Fu, G., Yuan, H., Wang, S., Gadda, G., Weber, I. T.
    Atomic-resolution structure of an N5 flavin adduct in D-arginine dehydrogenase.
    Biochemistry 50 : 6292-6294 (2011). [PMID: 21707047]
  6. Yuan, H., Xin, Y., Hamelberg, D., 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 : 18957-18965 (2011). [PMID: 21999550]

[EC created 1972 as EC, transferred 2015 to EC]