Glutamate dehydrogenase (NADP+)
| Glutamate dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.1.4 | ||||||||
| CAS no. | 2604121 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Glutamate dehydrogenase (NADP+) (EC 1.4.1.4, glutamic dehydrogenase, dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)), glutamic acid dehydrogenase, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, NAD(P)+-glutamate dehydrogenase, NAD(P)H-dependent glutamate dehydrogenase, glutamate dehydrogenase (NADP+)) is an enzyme with systematic name L-glutamate:NADP+ oxidoreductase (deaminating).[1][2][3][4] This enzyme catalyses the following chemical reaction
- L-glutamate + H2O + NADP+ 2-oxoglutarate + NH3 + NADPH + H+
References[edit]
- ^ Coulton JW, Kapoor M (April 1973). "Purification and some properties of the glutamate dehydrogenase of Salmonella typhimurium". Canadian Journal of Microbiology. 19 (4): 427–38. doi:10.1139/m73-071. PMID 4144743.
- ^ Grisolia S, Quijada CL, Fernandez M (1964). "Glutamate dehydrogenase from yeast and from animal tissues". Biochim. Biophys. Acta. 81: 61–70. doi:10.1016/0926-6569(64)90335-9.
- ^ Shiio I, Ozaki H (November 1970). "Regulation of nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase from Brevibacterium flavum, a glutamate-producing bacterium". Journal of Biochemistry. 68 (5): 633–47. PMID 4394939.
- ^ Smith, E.L.; Austen, B.M.; Blumenthal, K.M.; Nyc, J.F. (1975). "Glutamate dehydrogenases". In Boyer, P.D. (ed.). The Enzymes. Vol. 11 (3rd ed.). New York: Academic Press. pp. 293–367.
External links[edit]
- Glutamate+dehydrogenase+(NADP+) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
