EC 1.4.99.6 - D-arginine dehydrogenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.4.99.6

Names

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)

Reaction

Cofactor

Comments:

Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.1.25, 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
UniProtKB/Swiss-Prot:

References

  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 1.4.99.6 created 1972 as EC 1.4.99.1, transferred 2015 to EC 1.4.99.6]