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| EC | 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+ |
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| 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) | ||||||||
| Comments: | 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. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37213-53-9 | ||||||||
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