EC number:2.6.1.88
| ID: | 2.6.1.88 |
|---|---|
| Description: | Methionine transaminase. |
| Alternative Name: |
Methionine-oxo-acid transaminase. |
| Cath: | 3.40.640.10; 3.90.1150.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.6.1.88 |
| BRENDA Enzyme Link: | BRENDA 2.6.1.88 |
| KEGG Enzyme Link: | KEGG2.6.1.88 |
| BioCyc Enzyme Link: | BioCyc 2.6.1.88 |
| ExPASy Enzyme Link: | ExPASy2.6.1.88 |
| EC2PDB Enzyme Link: | EC2PDB 2.6.1.88 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.6.1.88 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.6.1.88 |
| IntEnz Enzyme Link: | IntEnz 2.6.1.88 |
| MEDLINE Enzyme Link: | MEDLINE 2.6.1.88 |
| RHEA:31763 | a 2-oxocarboxylate + L-methionine = 4-(methylsulfanyl)-2-oxobutanoate + an L-alpha-amino acid |
| 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 |
|---|---|---|---|
| Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function. | Dolzan M, Johansson K, Roig-Zamboni V, Campanacci V, Tegoni M, Schneider G, Cambillau C | 2004 Jul 30 | 15280032 |