ExplorEnz: EC 1.4.1.21

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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. [DOI] [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]