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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
EC Tree
1.4.1.6 created 1961, deleted 1982
1.97.1.5 created 2000 deleted 2001
1.97.1.6 created 2000 deleted 2001
1.97.1.7 created 2000, deleted 2001