ExplorEnz: EC 1.4.1.14

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1.4.1.14

Accepted name:

glutamate synthase (NADH)

Reaction:

2 L-glutamate + NAD⁺ = L-glutamine + 2-oxoglutarate + NADH + H⁺
(1a) L-glutamate + NH₃ = L-glutamine + H₂O
(1b) L-glutamate + NAD⁺ + H₂O = NH₃ + 2-oxoglutarate + NADH + H⁺

Other name(s):

glutamate (reduced nicotinamide adenine dinucleotide) synthase; NADH: GOGAT; L-glutamate synthase (NADH); L-glutamate synthetase; NADH-glutamate synthase; NADH-dependent glutamate synthase

Systematic name:

L-glutamate:NAD⁺ oxidoreductase (transaminating)

Comments:

A flavoprotein (FMN). The reaction takes place in the direction of L-glutamate production. The protein is composed of two domains, one hydrolysing L-glutamine to NH₃ and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH₃ with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.2, glutamate dehydrogenase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 65589-88-0

References:

1.	Roon, R.J., Even, H.L. and Larimore, F. Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae. J. Bacteriol. 118 (1974) 89–95. [PMID: 4362465]
2.	Boland, M.J. and Benny, A.G. Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules. Eur. J. Biochem. 79 (1977) 355–362. [DOI] [PMID: 21790]
3.	Masters, D.S., Jr. and Meister, A. Inhibition of homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae. J. Biol. Chem. 257 (1982) 8711–8715. [PMID: 7047525]
4.	Anderson, M.P., Vance, C.P., Heichel, G.H. and Miller, S.S. Purification and characterization of NADH-glutamate synthase from alfalfa root nodules. Plant Physiol. 90 (1989) 351–358. [PMID: 16666762]
5.	Blanco, L., Reddy, P.M., Silvente, S., Bucciarelli, B., Khandual, S., Alvarado-Affantranger, X., Sanchez, F., Miller, S., Vance, C. and Lara-Flores, M. Molecular cloning, characterization and regulation of two different NADH-glutamate synthase cDNAs in bean nodules. Plant Cell Environ. 31 (2008) 454–472. [PMID: 18182018]

[EC 1.4.1.14 created 1978, modified 2019]