EC number:1.4.1.14
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.4 Acting on the CH-NH2 group of donors |
| 1.4.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.4.1.14 | ||
|---|---|---|---|
| Description: | Glutamate synthase (NADH). | ||
| Alternative Name: |
NADH-glutamate synthase. NADH-dependent glutamate synthase. L-glutamate synthetase. L-glutamate synthase. | ||
| Prosite: | PDOC00406; | ||
| PDB: |
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3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.4.1.14 |
| BRENDA Enzyme Link: | BRENDA 1.4.1.14 |
| KEGG Enzyme Link: | KEGG1.4.1.14 |
| BioCyc Enzyme Link: | BioCyc 1.4.1.14 |
| ExPASy Enzyme Link: | ExPASy1.4.1.14 |
| EC2PDB Enzyme Link: | EC2PDB 1.4.1.14 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.4.1.14 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.4.1.14 |
| IntEnz Enzyme Link: | IntEnz 1.4.1.14 |
| MEDLINE Enzyme Link: | MEDLINE 1.4.1.14 |
| RHEA:13753 | 2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine + NADH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[*:13]=[C;H0;+0:14](-[*:15])-[OH;+0:16]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:16].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[*:13]=[C;H0;+0:14](-[*:15])-[NH2;+0:4] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae. | Roon RJ, Even HL, Larimore F | 1974 Apr | 4362465 |
| Kinetic mechanism of NADH-dependent glutamate synthase from lupin nodules. | Boland MJ | 1979 Sep | 227686 |
| Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules. | Boland MJ, Benny AG | 1977 Oct 3 | 21790 |
| Purification and Characterization of NADH-Glutamate Synthase from Alfalfa Root Nodules. | Anderson MP, Vance CP, Heichel GH, Miller SS | 1989 May | 16666762 |