1.4.99.6	malfunction	utilization of L-Ala, L-Trp, D-Ala, D-His, D-Phe, D-Ser, D-Thr, and D-Val as sole nitrogen sources is abolished in the dadA mutant	
1.4.99.6	metabolism	D-amino acid dehydrogenase activity of broad substrate specificity	
1.4.99.6	metabolism	DADH catalyzes an asynchronous CH and NH bond cleavage via a hydride transfer mechanism. The enzyme follows a ping-pong bibi mechanism. The shape and flexibility of loop L1 in the active site of DADH are important for substrate capture and broad substrate specificity	
1.4.99.6	physiological function	the enzyme is highly expressed by Pseudomonas aeruginosa within the cystic fibrosis lung, and it is required for optimal production of hydrogen cyanide by some cystic fibrosis-adapted isolates. The enzyme is required for optimal production of pyocyanin, pyoverdine, and rhamnolipid by cystic fibrosis-adapted and non-cystic fibrosis-adapted isolates of Pseudomonas aeruginosa. In addition, the enzyme is required for optimal production of alginate, biofilm formation, and virulence of a cystic fibrosis-adapted isolated of Pseudomonas aeruginosa	
1.4.99.6	physiological function	D-to-L inversion in D-arginine metabolism requires both D-arginine dehydrogenase DauA and NAD(P)H-dependent anabolic L-arginine dehydrogenase DauB. DauA catalyzes oxidative deamination of D-arginine into 2-oxoarginine and ammonia, and DauB is able to use 2-ketoarginine and ammonia as substrates and convert them into L-arginine in the presence of NADPH or NADH. DauA and DauB are coupled catabolic and anabolic dehydrogenases that enable D-arginine utilization through L-arginine catabolic pathways	
1.4.99.6	physiological function	involved in catabolism of several D-amino acids	
1.4.99.6	physiological function	proteins from the Rid2 and Rid3 subfamilies deaminate iminoarginine, generated in situ by D-arginine dehydrogenase DauA. DauA uses either a Rid protein or solvent water to generate a ketoacid. Rid proteins compete with semicarbazide for the iminoarginine product of the first reaction step