The Enzyme Database

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EC 1.4.1.21     
Accepted name: aspartate dehydrogenase
Reaction: L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+
Other name(s): NAD-dependent aspartate dehydrogenase; NADH2-dependent aspartate dehydrogenase; NADP+-dependent aspartate dehydrogenase
Systematic name: L-aspartate:NAD(P)+ oxidoreductase (deaminating)
Comments: The enzyme is strictly specific for L-aspartate as substrate. Catalyses the first step in NAD biosynthesis from aspartate. The enzyme has a higher affinity for NAD+ than NADP+ [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-97-0
References:
1.  Yang, Z., Savchenko, A., Yakunin, A., Zhang, R., Edwards, A., Arrowsmith, C. and Tong, L. Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J. Biol. Chem. 278 (2003) 8804–8808. [PMID: 12496312]
2.  Okamura, T., Noda, H., Fukuda, S. and Ohsugi, M. Aspartate dehydrogenase in vitamin B12-producing Klebsiella pneumoniae IFO 13541. J. Nutr. Sci. Vitaminol. 44 (1998) 483–490. [PMID: 9819709]
3.  Kretovich, W.L., Kariakina, T.I., Weinova, M.K., Sidelnikova, L.I. and Kazakova, O.W. The synthesis of aspartic acid in Rhizobium lupini bacteroids. Plant Soil 61 (1981) 145–156.
[EC 1.4.1.21 created 2005]
 
 


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