D-serine ammonia-lyase
| D-serine ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.18 | ||||||||
| CAS no. | 9015-88-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a D-serine ammonia-lyase (EC 4.3.1.18) is an enzyme that catalyzes the chemical reaction
- D-serine pyruvate + NH3
Hence, this enzyme has one substrate, D- in common use include D-hydroxyaminoacid dehydratase, D-serine dehydrase, D-hydroxy amino acid dehydratase, D-serine hydrolase, D-serine dehydratase (deaminating), D-serine deaminase, and D-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
References
- Dupourque D, Newton WA, Snell EE (1966). "Purification and properties of D-serine dehydrase from Escherichia coli". J. Biol. Chem. 241 (5): 1233–8. PMID 5327100.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - METZLER DE, SNELL EE (1952). "Deamination of serine. II. D-Serine dehydrase, a vitamin B6 enzyme from Escherichia coli". J. Biol. Chem. 198 (1): 363–73. PMID 12999751.