Biology:L-serine ammonia-lyase
From HandWiki
| L-serine ammonia-lyase | |||||||||
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 Serine dehydratase monomer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 4.3.1.17 | ||||||||
| 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 L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction
- L-serine = pyruvate + NH3 (overall reaction)
- (1a) L-serine = 2-aminoprop-2-enoate + H2O
- (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
- (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-serine ammonia-lyase (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine deaminase, L-serine dehydratase, and L-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine, threonine and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1P5J, 1PWE, 1PWH, and 2IQQ.
References
- "Occurrence of a catabolic L-serine (L-threonine) deaminase in Saccharomyces cerevisiae". Eur. J. Biochem. 123 (3): 571–6. 1982. doi:10.1111/j.1432-1033.1982.tb06570.x. PMID 7042346.
- "L-serine dehydratase from rat liver. Purification and some properties". Biochim. Biophys. Acta 321 (1): 361–8. 1973. doi:10.1016/0005-2744(73)90091-0. PMID 4750769.
- "L-Serine dehydratase (rat liver)". Methods Enzymol. 17B: 346–351. 1971. doi:10.1016/0076-6879(71)17060-7.
- "L-Serine dehydratase (Clostridium acidiurica)". Methods Enzymol. 17B: 351–356. 1971. doi:10.1016/0076-6879(71)17061-9.
- "L-Serine dehydratase (Escherichia coli)". Methods Enzymol. 17B: 356–360. 1971. doi:10.1016/0076-6879(71)17062-0.
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