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EC 1.4.1.13 Details
EC number
1.4.1.13
Accepted name
glutamate synthase (NADPH)
Reaction
2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+ (overall reaction);;(1a) L-glutamate + NH3 = L-glutamine + H2O;;(1b) L-glutamate + NADP+ + H2O = NH3 + 2-oxoglutarate + NADPH + H+
Other name(s)
glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase, L-glutamate synthase, L-glutamate synthetase, glutamate synthetase (NADP), NADPH-dependent glutamate synthase, glutamine-ketoglutaric aminotransferase, NADPH-glutamate synthase, NADPH-linked glutamate synthase, glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP), L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing, GOGAT
Systematic name
L-glutamate:NADP+ oxidoreductase (transaminating)
CAS registry number
37213-53-9
Comment
Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the direction of L-glutamate production. The protein is composed of two subunits, α and β. The α subunit 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 1.4.1.4, glutamate dehydrogenase [NADP+]). The β subunit transfers electrons from the cosubstrate. The NH3 is channeled within the α subunit through a 31 Å channel. The chanelling is very efficient and in the intact α-β complex ammonia is produced only within the complex. In the absence of the β subunit, coupling between the two domains of the α subunit is compromised and some ammonium can leak.
History
created 1972 as EC 2.6.1.53, transferred 1976 to EC 1.4.1.13, modified 2001, modified 2012