ExplorEnz: EC 1.4.1.4

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1.4.1.4

Accepted name:

glutamate dehydrogenase (NADP⁺)

Reaction:

L-glutamate + H₂O + NADP⁺ = 2-oxoglutarate + NH₃ + NADPH + H⁺ (overall reaction)
(1a) 2-iminoglutarate + H₂O = 2-oxoglutarate + NH₃
(1b) L-glutamate + NADP⁺ = 2-iminoglutarate + NADPH

Other name(s):

glutamic dehydrogenase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)⁺-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase

Systematic name:

L-glutamate:NADP⁺ oxidoreductase (deaminating)

Comments:

The enzyme plays an important role in the interconversion of nitrogen and carbon metabolism. The reaction starts by conversion of 2-oxoglutarate to 2-iminoglutarate through a nucleophilic attack by ammonia, and continues with reduction by NADPH to yield glutamate. The NADP-dependent enzyme plays a role in ammonia anabolism. A related NAD-dependent enzyme [EC 1.4.1.2, glutamate dehydrogenase (NAD⁺)] is generally involved in the degradation of glutamate into 2-oxoglutarate and ammonia. Some enzymes show dual co-substrate specificity (EC 1.4.1.3, glutamate dehydrogenase [NAD(P)⁺]).

Links to other databases:

BRENDA, EXPASY, GENE, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9029-11-2

References:

1.	Coulton, J.W. and Kapoor, M. Purification and some properties of the glutamate dehydrogenase of Salmonella typhimurium. Can. J. Microbiol. 19 (1973) 427–438. [DOI] [PMID: 4144743]
2.	Grisolia, S., Quijada, C.L. and Fernandez, M. Glutamate dehydrogenase from yeast and from animal tissues. Biochim. Biophys. Acta 81 (1964) 61–70. [DOI]
3.	Shiio, I. and Ozaki, H. Regulation of nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase from Brevibacterium flavum, a glutamate-producing bacterium. J. Biochem. (Tokyo) 68 (1970) 633–647. [DOI] [PMID: 4394939]
4.	Hochreiter, M.C., Patek, D.R. and Schellenberg, K.A. Catalysis of α-iminoglutarate formation from α-ketoglutarate and ammonia by bovine glutamate dehydrogenase. J. Biol. Chem. 247 (1972) 6271–6276. [DOI] [PMID: 4346809]
5.	Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F. Glutamate dehydrogenases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 293–367.
6.	Fisher, H.F. and Viswanathan, T.S. Carbonyl oxygen exchange evidence of imine formation in the glutamate dehydrogenase reaction and identification of the "occult role" of NADPH. Proc. Natl. Acad. Sci. USA 81 (1984) 2747–2751. [DOI] [PMID: 6144102]
7.	Srinivasan, R., Viswanathan, T.S. and Fisher, H.F. Mechanism of formation of bound α-iminoglutarate from α-ketoglutarate in the glutamate dehydrogenase reaction. A chemical basis for ammonia recognition. J. Biol. Chem. 263 (1988) 2304–2308. [DOI] [PMID: 3339011]
8.	Tomita, T., Yin, L., Nakamura, S., Kosono, S., Kuzuyama, T. and Nishiyama, M. Crystal structure of the 2-iminoglutarate-bound complex of glutamate dehydrogenase from Corynebacterium glutamicum. FEBS Lett. 591 (2017) 1611–1622. [DOI] [PMID: 28486765]

[EC 1.4.1.4 created 1961]