EC number:2.6.1.9
| ID: | 2.6.1.9 | ||
|---|---|---|---|
| Description: | Histidinol-phosphate transaminase. | ||
| Alternative Name: |
Imidazolylacetolphosphate aminotransferase. Imidazole acetol-phosphate transaminase. Histidinol-phosphate aminotransferase. | ||
| Prosite: | PDOC00518; | ||
| PDB: |
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||
| Cath: | 3.40.640.10; 3.90.1150.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.6.1.9 |
| BRENDA Enzyme Link: | BRENDA 2.6.1.9 |
| KEGG Enzyme Link: | KEGG2.6.1.9 |
| BioCyc Enzyme Link: | BioCyc 2.6.1.9 |
| ExPASy Enzyme Link: | ExPASy2.6.1.9 |
| EC2PDB Enzyme Link: | EC2PDB 2.6.1.9 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.6.1.9 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.6.1.9 |
| IntEnz Enzyme Link: | IntEnz 2.6.1.9 |
| MEDLINE Enzyme Link: | MEDLINE 2.6.1.9 |
| RHEA:23744 | 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate |
| 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 |
|---|---|---|---|
| Insights into the structural basis of substrate recognition by histidinol-phosphate aminotransferase from Corynebacterium glutamicum. | Marienhagen J, Sandalova T, Sahm H, Eggeling L, Schneider G | 2008 Jun | 18560156 |
| Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase. | Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M | 2004 May 14 | 15007066 |
| Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate. | Sivaraman J, Li Y, Larocque R, Schrag JD, Cygler M, Matte A | 2001 Aug 24 | 11518529 |