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 | Maltose regulon modulator MalY |
Enzyme Information
| 4.4.1.8 |
Cystathionine beta-lyase.
based on mapping to UniProt P23256
L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate.
-!- The enzyme cleaves a carbon-sulfur bond, releasing L-homocysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds. -!- Possibly identical, in Saccharomyces cerevisiae, with EC 4.4.1.6.
|
UniProtKB Entries (1)
| P23256 |
MALY_ECOLI
Escherichia coli K-12
Protein MalY
|
PDB Structure
| PDB | 1D2F |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.
EMBO J.
|
