Glutamate dehydrogenase (NAD(P)+)
Glutamate dehydrogenase (NAD(P)+) | |||||||||
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glutamate dehydrogenase hexamer, Human | |||||||||
Identifiers | |||||||||
EC number | 1.4.1.3 | ||||||||
CAS number | 2604152 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Glutamate dehydrogenase (NAD(P)+) (EC 1.4.1.3, glutamic dehydrogenase, glutamate dehydrogenase [NAD(P)+]) is an enzyme with systematic name L-glutamate:NAD(P)+ oxidoreductase (deaminating).[1][2][3] This enzyme catalyses the following chemical reaction
- L-glutamate + H2O + NAD(P)+ 2-oxoglutarate + NH3 + NAD(P)H + H+
References
- ↑ Olson, J.A.; Anfinsen, C.B. (1952). "The crystallization and characterization of L-glutamic acid dehydrogenase". J. Biol. Chem. 197: 67–79. PMID 12981035.
- ↑ Smith, E.L.; Austen, B.M.; Blumenthal, K.M.; Nyc, J.F. (1975). "Glutamate dehydrogenases". In Boyer, P.D. The Enzymes. 11 (3rd ed.). New York: Academic Press. pp. 293–367.
- ↑ Strecker, H.J. (1953). "Glutamic dehydrogenase". Arch. Biochem. Biophys. 46: 128–140. PMID 13092953.
External links
- Glutamate dehydrogenase (NAD(P) ) at the US National Library of Medicine Medical Subject Headings (MeSH)
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