D-octopine dehydrogenase

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In enzymology, a D-octopine dehydrogenase (EC 1.5.1.11) is an enzyme that catalyzes the chemical reaction

N₂-(D-1-carboxyethyl)-L-arginine + NAD⁺ + H₂O $\rightleftharpoons$ L-arginine + pyruvate + NADH + H⁺

The 3 substrates of this enzyme are N2-(D-1-carboxyethyl)-L-arginine, NAD⁺, and H₂O, whereas its 4 products are L-arginine, pyruvate, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase (L-arginine-forming). Other names in common use include D-octopine synthase, octopine dehydrogenase, octopine:NAD+ oxidoreductase, ODH, 2-N-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase, and (L-arginine-forming). This enzyme participates in arginine and proline metabolism.

[edit] References

IUBMB entry for 1.5.1.11
BRENDA references for 1.5.1.11 (Recommended.)
PubMed references for 1.5.1.11
PubMed Central references for 1.5.1.11
Google Scholar references for 1.5.1.11
Kemp JD, Hack E, Sutton DW and El-Wakil M (1979). "Unusual amino acids and their relationship to tumorigenesis". Proc. Int. Conf. Plant Pathol. Bact. 4th: 183–188.
van Thoai N, Huc C, Pho DB, Olomucki A (1969). "[Octopine dehydrogenase. Purification and catalytic properties]". Biochim. Biophys. Acta. 191: 46–57. PMID 4310628.