CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.640 | Aspartate Aminotransferase; domain 2 |
|
3.40.640.10 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
Domain Context
CATH Clusters
| Superfamily | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
| Functional Family | Aspartate aminotransferase |
Enzyme Information
| 2.6.1.88 |
Methionine transaminase.
based on mapping to UniProt P77806
L-methionine + a 2-oxo acid = 2-oxo-4-methylthiobutanoate + an L-amino acid.
-!- The enzyme is most active with L-methionine. -!- It participates in the L-methionine salvage pathway from S-methyl- 5'-thioadenosine, a by-product of polyamine biosynthesis. -!- The enzyme from the bacterium Klebsiella pneumoniae can use several different amino acids as amino donor, with aromatic amino acids being the most effective. -!- The enzyme from the plant Arabidopsis thaliana is also a part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates.
|
UniProtKB Entries (1)
| P77806 |
YBDL_ECOLI
Escherichia coli K-12
Methionine aminotransferase
|
PDB Structure
| PDB | 1U08 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function
FEBS Lett.
|
