IUBMB Enzyme Nomenclature


Accepted name: aspartate dehydrogenase

Reaction: L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+ (overall reaction)
(1a) L-aspartate + NAD(P)+ = 2-iminosuccinate + NAD(P)H + H+
(1b) 2-iminosuccinate + H2O = oxaloacetate + NH3 (spontaneous)

Other name(s): AspDH; NAD-dependent aspartate dehydrogenase; NADH2-dependent aspartate dehydrogenase; NADP+-dependent aspartate dehydrogenase; nadX (gene name); L-aspartate:NAD(P)+ oxidoreductase (deaminating)

Systematic name: L-aspartate:NAD(P)+ oxidoreductase (2-iminosuccinate-forming)

Comments: The enzyme is strictly specific for L-aspartate as substrate. It produces the unstable compound 2-iminosuccinate, which, in the presence of water, hydrolyses spontaneously to form oxaloacetate. The enzyme from some archaea and thermophilic bacteria is likely to transfer 2-iminosuccinate directly to EC, quinolinate synthase, preventing its hydrolysis and enabling the de novo biosynthesis of NAD+.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-97-0


1. 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.

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. 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]

4. Yoneda, K., Kawakami, R., Tagashira, Y., Sakuraba, H., Goda, S. and Ohshima, T. The first archaeal L-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: gene cloning and enzymological characterization. Biochim. Biophys. Acta 1764 (2006) 1087-1093. [PMID: 16731057]

5. Yoneda, K., Sakuraba, H., Tsuge, H., Katunuma, N. and Ohshima, T. Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex. FEBS J. 274 (2007) 4315-4325. [PMID: 17651440]

6. Li, Y., Kawakami, N., Ogola, H.J., Ashida, H., Ishikawa, T., Shibata, H. and Sawa, Y. A novel L-aspartate dehydrogenase from the mesophilic bacterium Pseudomonas aeruginosa PAO1: molecular characterization and application for L-aspartate production. Appl. Microbiol. Biotechnol. 90 (2011) 1953-1962. [PMID: 21468714]

7. Li, Y., Ishida, M., Ashida, H., Ishikawa, T., Shibata, H. and Sawa, Y. A non-NadB type L-aspartate dehydrogenase from Ralstonia eutropha strain JMP134: molecular characterization and physiological functions. Biosci. Biotechnol. Biochem. 75 (2011) 1524-1532. [PMID: 21821928]

8. Li, Y., Ogola, H.J. and Sawa, Y. L-aspartate dehydrogenase: features and applications. Appl. Microbiol. Biotechnol. 93 (2012) 503-516. [PMID: 22120624]

[EC created 2005, modified 2022]

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