1.4.99.6: D-arginine dehydrogenase
This is an abbreviated version!
For detailed information about D-arginine dehydrogenase, go to the full flat file.
Reaction
Synonyms
D-alanine dehydrogenase, D-amino acid dehydrogenase, D-amino acid dehydrogenase DadA, DAADH, DAD, DadA, DADH, DauA, EC 1.4.99.1, NADP+-dependent D-amino acid dehydrogenase
ECTree
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General Information
General Information on EC 1.4.99.6 - D-arginine dehydrogenase
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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
metabolism
physiological function
D-amino acid dehydrogenase activity of broad substrate specificity
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
metabolism
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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
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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
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
physiological function
involved in catabolism of several D-amino acids
physiological function
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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