Aspartate dehydrogenase

Aspartate dehydrogenase (EC 1.4.1.21) is an enzyme that catalyzes the chemical reaction

Aspartate dehydrogenase
Identifiers
EC no.1.4.1.21
CAS no.37278-97-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins
L-aspartate + H2O + NAD(P)+ oxaloacetate + NH3 + NAD(P)H + H+

The 4 substrates of this enzyme are L-aspartate, water, nicotinamide adenine dinucleotide ion, and nicotinamide adenine dinucleotide phosphate ion, whereas its 5 products are oxaloacetate, ammonia, NADH, nicotinamide adenine dinucleotide phosphate, and hydrogen ion.

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.

Structural studies

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

References

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  • Tong L; Savchenko, A; Yakunin, A; Zhang, R; Edwards, A; Arrowsmith, C; Tong, L (2003). "Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643". J. Biol. Chem. 278 (10): 8804–8. doi:10.1074/jbc.M211892200. PMID 12496312.
  • Okamura T, Noda H, Fukuda S, Ohsugi M (August 1998). "Aspartate dehydrogenase in vitamin B12-producing Klebsiella pneumoniae IFO 13541". J. Nutr. Sci. Vitaminol. 44 (4). Tokyo: 483–90. doi:10.3177/jnsv.44.483. PMID 9819709.
  • Kazakova OW; Kariakina, T. I.; Weinova, M. K.; Sidelnikova, L. I.; Kazakova, O. W. (1981). "The synthesis of aspartic acid in Rhizobium lupini bacteroids". Plant Soil. 61 (1–2): 145–156. Bibcode:1981PlSoi..61..145K. doi:10.1007/BF02277371. S2CID 44867070.