CATH Classification

Domain Context

CATH Clusters

Superfamily FAD/NAD(P)-binding domain
Functional Family

Enzyme Information

1.4.99.6
D-arginine dehydrogenase.
based on mapping to UniProt Q9HXE3
D-arginine + acceptor + H(2)O = 5-guanidino-2-oxopentanoate + NH(3) + reduced acceptor.
-!- The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.1.25 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. -!- Formerly EC 1.4.99.1.

UniProtKB Entries (1)

Q9HXE3
DAUA_PSEAE
Pseudomonas aeruginosa PAO1
FAD-dependent catabolic D-arginine dehydrogenase DauA

PDB Structure

PDB 3NYE
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase.
Fu, G., Yuan, H., Li, C., Lu, C.D., Gadda, G., Weber, I.T.
Biochemistry