D-serine ammonia-lyase
Appearance
D-serine ammonia-lyase | |||||||||
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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 | ||||||||
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The enzyme D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), catalyzes the chemical reaction
- D-serine = pyruvate + NH3 (overall reaction)
- (1a) D-serine = 2-aminoprop-2-enoate + H2O
- (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
- (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous
Other names 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
[edit]- Dupourque D, Newton WA, Snell EE (1966). "Purification and properties of D-serine dehydrase from Escherichia coli". J. Biol. Chem. 241 (5): 1233–8. doi:10.1016/S0021-9258(18)96825-0. PMID 5327100.
- 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. doi:10.1016/S0021-9258(18)55590-3. PMID 12999751.