Aspartate dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, an aspartate dehydrogenase (EC 1.4.1.21) is an enzyme that catalyzes the chemical reaction

L-aspartate + H₂O + NAD(P)+ $\rightleftharpoons$ oxaloacetate + NH₃ + NAD(P)H + H⁺

The 4 substrates of this enzyme are L-aspartate, H₂O, NAD⁺, and NADP⁺, whereas its 5 products are oxaloacetate, NH₃, NADH, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-aspartate:NAD(P)+ oxidoreductase (deaminating). Other names in common use include NAD-dependent aspartate dehydrogenase, NADH2-dependent aspartate dehydrogenase, and NADP+-dependent aspartate dehydrogenase. This enzyme participates in nicotinate and nicotinamide metabolism.

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2DC1.

[edit] References

IUBMB entry for 1.4.1.21
BRENDA references for 1.4.1.21 (Recommended.)
PubMed references for 1.4.1.21
PubMed Central references for 1.4.1.21
Google Scholar references for 1.4.1.21
Tong L (2003). "Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643". J. Biol. Chem. 278: 8804–8. doi:10.1074/jbc.M211892200. PMID 12496312.
Okamura T, Noda H, Fukuda S, Ohsugi M (Tokyo). "Aspartate dehydrogenase in vitamin B12-producing Klebsiella pneumoniae IFO 13541". J. Nutr. Sci. Vitaminol.: 483–90. PMID 9819709.
and Kazakova OW (1981). "The synthesis of aspartic acid in Rhizobium lupini bacteroids". Plant Soil 61: 145–156. doi:10.1007/BF02277371.