EC number:2.6.1.18
| ID: | 2.6.1.18 |
|---|---|
| Description: | Beta-alanine--pyruvate transaminase. |
| Alternative Name: |
Omega-amino acid--pyruvate aminotransferase. Beta-alanine--pyruvate aminotransferase. |
| Cath: | 3.40.640.10; 3.90.1150.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.6.1.18 |
| BRENDA Enzyme Link: | BRENDA 2.6.1.18 |
| KEGG Enzyme Link: | KEGG2.6.1.18 |
| BioCyc Enzyme Link: | BioCyc 2.6.1.18 |
| ExPASy Enzyme Link: | ExPASy2.6.1.18 |
| EC2PDB Enzyme Link: | EC2PDB 2.6.1.18 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.6.1.18 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.6.1.18 |
| IntEnz Enzyme Link: | IntEnz 2.6.1.18 |
| MEDLINE Enzyme Link: | MEDLINE 2.6.1.18 |
| RHEA:14077 | 3-oxopropanoate + L-alanine = beta-alanine + pyruvate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[CH;+0:6]=[O;H0;+0:7]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:7].[*:5]-[CH2;+0:6]-[NH2;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Properties of the bound coenzyme and subunit structure of omega-amino acid:pyruvate aminotransferase. | Yonaha K, Toyama S, Kagamiyama H | 1983 Feb 25 | 6822556 |
| Structural studies of Pseudomonas and Chromobacterium ω-aminotransferases provide insights into their differing substrate specificity. | Sayer C, Isupov MN, Westlake A, Littlechild JA | 2013 Apr | 23519665 |
| Functional characterization of seven γ-Glutamylpolyamine synthetase genes and the bauRABCD locus for polyamine and β-Alanine utilization in Pseudomonas aeruginosa PAO1. | Yao X, He W, Lu CD | 2011 Aug | 21622750 |