EC number:2.6.1.15
| ID: | 2.6.1.15 |
|---|---|
| Description: | Glutamine--pyruvate transaminase. |
| Alternative Name: |
Glutamine--pyruvate aminotransferase. Glutamine--oxo-acid transaminase. Glutamine transaminase L. Glutaminase II. |
| Cath: | 3.40.640.10; 3.90.1150.10; |
3D structure
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 2.6.1.15 |
| BRENDA Enzyme Link: | BRENDA 2.6.1.15 |
| KEGG Enzyme Link: | KEGG2.6.1.15 |
| BioCyc Enzyme Link: | BioCyc 2.6.1.15 |
| ExPASy Enzyme Link: | ExPASy2.6.1.15 |
| EC2PDB Enzyme Link: | EC2PDB 2.6.1.15 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.6.1.15 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.6.1.15 |
| IntEnz Enzyme Link: | IntEnz 2.6.1.15 |
| MEDLINE Enzyme Link: | MEDLINE 2.6.1.15 |
| RHEA:10400 | L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[CH;+0:6](-[*:7])-[NH2;+0:8]>>[*:5]-[C;H0;+0:6](-[*:7])=[O;H0;+0:4].[*:1]-[CH;+0:2](-[*:3])-[NH2;+0:8] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Isolation and properties of highly purified glutamine transaminase. | Cooper JL, Meister A | 1972 Feb 29 | 5059882 |
| Studies on the mechanism and specificity of the glutamine-alpha-keto acid transamination-deamidation reaction. | MEISTER A | 1954 Sep | 13201566 |