|
|
| |
4.3.1.18 |
| Description |
D-serine ammonia-lyase |
| Alternative names |
D-serine dehydratase;
D-serine dehydrase;
D-hydroxy amino acid dehydratase;
D-serine hydrolase;
D-serine dehydratase (deaminating);
D-serine deaminase;
D-serine hydro-lyase (deaminating).
|
| Catalyzed reaction |
D-serine = pyruvate + NH(3). |
| Cofactor |
Pyridoxal-phosphate or Zn(II) ions plus pyridoxal-phosphate. |
| Comments |
Also acts, slowly, on D-threonine.
The reaction catalyzed probably involves initial elimination of water (hence the enzyme's original classification as EC 4.2.1.14),followed by isomerization and hydrolysis of the product with C-N bond breakage.
Formerly EC 4.2.1.14. |
| |
The enzyme from E. coli is a fold-type II protein, whereas the D-ser dehydratase from S. cerevisiae is a fold-type III enzyme and employs zinc ions as cofactors, in addition to pyridoxal phosphate. |
| PDB |
3SS7; 3SS9; |
| Organisms |
-Eubacteria -Fungi -Metazoa |
| | |
|---|
Family |
|
| | |
|---|
| Links |
Enzyme (activities) 4.3.1.18
BRENDA (activities) 4.3.1.18
KEGG (pathways) 4.3.1.18
PLPMDB (PLP mutants) 4.3.1.18
|
| | |
|---|
| References |
Articles on 4.3.1.18 |
| | |
|---|
| last changed |
2019/06/20 13:01 |
|
Browse:
Analyse:
Find: