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By constantly striving for products of utmost quality, Creative Enzymes has emerged as a worldwide leader in the field of enzyme activity assay. We are proud to provide the most reliable and precise methods for the activity measurement of D-arginine dehydrogenase.
D-arginine dehydrogenase (EC 1.4.99.6) was first discovered in 1972 as a D-amino acid dehydrogenase (EC 1.4.99.1), and later re-classified to EC 1.4.99.6 in 2015. D-arginine dehydrogenase is a novel flavin-dependent enzyme with FAD as a cofactor. This enzyme was isolated from bacterium Pseudomonas aeruginosa PAO1, a Gram-negative soil bacterium which is well-known to be a pivotal opportunistic human pathogen. D-arginine dehydrogenase is a catabolic enzyme that catalyzes the oxidative deamination of D-arginine to iminoarginine, which is nonenzymatically hydrolyzed to α-ketoarginine and ammonia. The two products are then converted to L-arginine by an anabolic L-arginine dehydrogenase. So the proposed physiological function of D-arginine dehydrogenase in Pseudomonas is to contribute to the first stage in a two-enzyme-coupled racemization of D-arginine to L-arginine. D-arginine dehydrogenase is a member of the general oxidoreductase family, that catalyzes the CH-OH group of the substrate and uses NAD+ or NADP+ as the cofactor. The systematic name of this enzyme is D-arginine:acceptor oxidoreductase (deaminating), which is also known as D-amino-acid:(acceptor) oxidoreductase (deaminating), D-amino-acid dehydrogenase or D-amino-acid:acceptor oxidoreductase (deaminating).
D-arginine dehydrogenase is active with a broad range of substrates, being capable of oxidizing D-amino acids of different size and polarity. All naturally occurring D-amino acids and glycine can be oxidized by this enzyme, with the exception of D-glutamate and D-aspartate. The physiological substrate, D-arginine, displays the highest activity. Unfortunately, activity assays of D-arginine dehydrogenase using spectrophotometry have not been well established on an industrial scale, although activity measurement using other methods has been reported before. The spectrophotometric assay is considered to be a reliable and cost-effective method for activity quantification. Today, Creative Enzymes is the leading company in the field of enzyme activity assays, which is well known to deliver the best customer satisfaction with the shortest product lead time. In short, Creative Enzymes promises to sustain professional standard and efficient services to continue to be your trustworthy partner.
Figure: The crystal structure of P. aeruginosa D-arginine dehydrogenase.
PDB: 3NYC
