ENZYME entry: EC 1.4.1.13
| Accepted Name |
| Glutamate synthase (NADPH).
|
| Alternative Name(s) |
| Glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase. |
| Glutamate synthetase (NADP). |
| Glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP). |
| Glutamine-ketoglutaric aminotransferase. |
| GOGAT. |
| L-glutamate synthase. |
| L-glutamate synthetase. |
| L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing. |
| NADPH-dependent glutamate synthase. |
| NADPH-glutamate synthase. |
| Reaction catalysed |
| 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH |
| Cofactor(s) |
| FAD; FMN; Iron-sulfur.
|
| Comment(s) |
- The reaction takes place in the opposite direction.
- The protein is composed of two subunits, alpha and beta.
- The alpha subunit is composed of two domains, one hydrolyzing
L-glutamine to NH(3) and L-glutamate (cf. EC 3.5.1.2), the other
combining the produced NH(3) with 2-oxoglutarate to produce a second
molecule of L-glutamate (cf. EC 1.4.1.4).
- The beta subunit transfers electrons to the cosubstrate.
- The NH(3) is channeled through a 31 A channel in the active protein.
- In the absence of the beta subunit, coupling between the two domains
of the alpha subunit is compromised and some ammonium can be
produced.
- In the intact alpha-beta complex, ammonia production only takes place
as part of the overall reaction.
- Formerly EC 2.6.1.53.
|
| Cross-references |
| PROSITE | PDOC00406 |
| BRENDA | 1.4.1.13 |
| EC2PDB | 1.4.1.13 |
| ExplorEnz | 1.4.1.13 |
| PRIAM enzyme-specific profiles | 1.4.1.13 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.4.1.13 |
| IUBMB Enzyme Nomenclature | 1.4.1.13 |
| IntEnz | 1.4.1.13 |
| MEDLINE | Find literature relating to 1.4.1.13 |
| MetaCyc | 1.4.1.13 |
| UniProtKB/Swiss-Prot |
| O29309, AGLUS_ARCFU; | Q3Z7F6, AGLUS_DEHE1; | Q58746, AGLUS_METJA; |
| Q9WYM8, AGLUS_THEMA; | B9KBQ2, AGLUS_THENN; | B1L993, AGLUS_THESQ; |
| Q9C102, GLT1_SCHPO; | P39812, GLTA_BACSU; | Q05755, GLTB_AZOBR; |
| O34399, GLTB_BACSU; | P09831, GLTB_ECOLI; | P96218, GLTB_MYCTU; |
| Q05756, GLTD_AZOBR; | P09832, GLTD_ECOLI; | P96219, GLTD_MYCTU; |
| O08340, GLTD_RHOSH; |
|
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