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EC 1.4.1.13 Details
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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 to the cosubstrate. The NH3 is channeled through a 31 Å channel in the active protein. In the absence of the β subunit, coupling between the two domains of the α subunit is compromised and some ammonium can be produced. In the intact alphaβ complex, ammonia production only takes place as part of the overall reaction.
History
created 1972 as EC 2.6.1.53, transferred 1976 to EC 1.4.1.13, modified 2001, modified 2012
EC Browser
1 Oxidoreductases (9651 organisms) download 3869963 sequences with EC number 1 in fasta format download 3869963 sequences with EC number 1 as tabstop The data in BRENDA allow the calculation or simulation of metabolic pathways by extracting the information of substrate/product chains and the corresponding kinetic data of the preceding and following enzymes in the Boehringer and KEGG metabolism (with the risk of including ?pathways? with non-natural compounds). version Download 2822 PDB numbers (EC 1) as tabstop separated file
1.4.1.6 created 1961, deleted 1982 show the reaction
2 Transferases (6622 organisms) download 6047191 sequences with EC number 2 in fasta format download 6047191 sequences with EC number 2 as tabstop The data in BRENDA allow the calculation or simulation of metabolic pathways by extracting the information of substrate/product chains and the corresponding kinetic data of the preceding and following enzymes in the Boehringer and KEGG metabolism (with the risk of including ?pathways? with non-natural compounds). version Download 2822 PDB numbers (EC 2) as tabstop separated file
3 Hydrolases (10604 organisms) download 3219244 sequences with EC number 3 in fasta format download 3219244 sequences with EC number 3 as tabstop The data in BRENDA allow the calculation or simulation of metabolic pathways by extracting the information of substrate/product chains and the corresponding kinetic data of the preceding and following enzymes in the Boehringer and KEGG metabolism (with the risk of including ?pathways? with non-natural compounds). version Download 2822 PDB numbers (EC 3) as tabstop separated file
4 Lyases (5111 organisms) download 1852335 sequences with EC number 4 in fasta format download 1852335 sequences with EC number 4 as tabstop The data in BRENDA allow the calculation or simulation of metabolic pathways by extracting the information of substrate/product chains and the corresponding kinetic data of the preceding and following enzymes in the Boehringer and KEGG metabolism (with the risk of including ?pathways? with non-natural compounds). version Download 2822 PDB numbers (EC 4) as tabstop separated file
5 Isomerases (2083 organisms) download 1146532 sequences with EC number 5 in fasta format download 1146532 sequences with EC number 5 as tabstop The data in BRENDA allow the calculation or simulation of metabolic pathways by extracting the information of substrate/product chains and the corresponding kinetic data of the preceding and following enzymes in the Boehringer and KEGG metabolism (with the risk of including ?pathways? with non-natural compounds). version Download 2822 PDB numbers (EC 5) as tabstop separated file
6 Ligases (1547 organisms) download 1713431 sequences with EC number 6 in fasta format download 1713431 sequences with EC number 6 as tabstop The data in BRENDA allow the calculation or simulation of metabolic pathways by extracting the information of substrate/product chains and the corresponding kinetic data of the preceding and following enzymes in the Boehringer and KEGG metabolism (with the risk of including ?pathways? with non-natural compounds). version Download 2822 PDB numbers (EC 6) as tabstop separated file
7 Translocases (966 organisms) download 592568 sequences with EC number 7 in fasta format download 592568 sequences with EC number 7 as tabstop The data in BRENDA allow the calculation or simulation of metabolic pathways by extracting the information of substrate/product chains and the corresponding kinetic data of the preceding and following enzymes in the Boehringer and KEGG metabolism (with the risk of including ?pathways? with non-natural compounds). version Download 2822 PDB numbers (EC 7) as tabstop separated file