Information on EC 1.4.99.6 - D-arginine dehydrogenase

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EC Tree 1 Oxidoreductases 1.4 Acting on the CH-NH₂ group of donors 1.4.99 With unknown physiological acceptors 1.4.99.6 D-arginine dehydrogenase

IUBMB 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.

The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

1.4.99.6
racemase
d-histidine
meso-diaminopimelate
d-leucine
d-methionine
d-isoleucine
ureibacillus
beta-chloro-d-alanine
walsh
d-tryptophan

Reaction Schemes

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D-arginine

acceptor

H2O

5-guanidino-2-oxopentanoate

NH3

reduced acceptor

Synonyms
d-amino acid dehydrogenase, d-alanine dehydrogenase, d-arginine dehydrogenase, daadh, d-amino acid dehydrogenase dada, nadp+-dependent d-amino acid dehydrogenase, more