Aspartate dehydrogenase
| Aspartate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.1.21 | ||||||||
| CAS no. | 37278-97-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Aspartate dehydrogenase (EC 1.4.1.21) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are L-aspartic acid, water, and oxidised nicotinamide adenine dinucleotide (NAD+}. Its products are oxaloacetic acid, ammonia, reduced NADH, and a proton. Nicotinamide adenine dinucleotide phosphate can be used as an alternative cofactor.[1][2][3]
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.[4]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2DC1.
References
- ^ Enzyme 1.4.1.21 at KEGG Pathway Database.
- ^ 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.
- ^ 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.