L-serine ammonia-lyase

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L-serine ammonia-lyase
1p5j.jpg
Serine dehydratase monomer, Human
Identifiers
EC no.4.3.1.17
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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[edit]

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1P5J, 1PWE, 1PWH, and 2IQQ.

References[edit]

  • Ramos F, Wiame JM (1982). "Occurrence of a catabolic L-serine (L-threonine) deaminase in Saccharomyces cerevisiae". Eur. J. Biochem. 123 (3): 571–6. doi:10.1111/j.1432-1033.1982.tb06570.x. PMID 7042346.
  • Simon D, Hoshino J, Kroger H (1973). "L-serine dehydratase from rat liver. Purification and some properties". Biochim. Biophys. Acta. 321 (1): 361–8. doi:10.1016/0005-2744(73)90091-0. PMID 4750769.
  • Suda M, Nakagawa H (1971). "L-Serine dehydratase (rat liver)". Methods Enzymol. 17B: 346–351. doi:10.1016/0076-6879(71)17060-7.
  • Sagers RD, Carter JE (1971). "L-Serine dehydratase (Clostridium acidiurica)". Methods Enzymol. 17B: 351–356. doi:10.1016/0076-6879(71)17061-9.
  • Robinson WG, Labow R (1971). "L-Serine dehydratase (Escherichia coli)". Methods Enzymol. 17B: 356–360. doi:10.1016/0076-6879(71)17062-0.