L-serine ammonia-lyase

From Wikipedia, the free encyclopedia

In enzymology, a L-serine ammonia-lyase (EC 4.3.1.17) is an enzyme that catalyzes the chemical reaction

L-serine $\rightleftharpoons$ pyruvate + NH₃

Hence, this enzyme has one substrate, L-serine, and two products, pyruvate and NH₃.

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 and threonine metabolism and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 4.3.1.17
BRENDA references for 4.3.1.17 (Recommended.)
PubMed references for 4.3.1.17
PubMed Central references for 4.3.1.17
Google Scholar references for 4.3.1.17
Ramos F, Wiame JM (1982). "Occurrence of a catabolic L-serine (L-threonine) deaminase in Saccharomyces cerevisiae". Eur. J. Biochem. 123: 571–6. PMID 7042346.
Simon D, Hoshino J, Kroger H (1973). "L-serine dehydratase from rat liver. Purification and some properties". Biochim. Biophys. Acta. 321: 361–8. PMID 4750769.
Suda M and Nakagawa H (1971). "L-Serine dehydratase (rat liver)". Methods Enzymol. 17B: 346–351.
Sagers RD and Carter J (1971). "E. L-Serine dehydratase (Clostridium acidiurica)". Methods Enzymol. 17B: 351–356.
Robinson WG and Labow R (1971). "L-Serine dehydratase (Escherichia coli)". Methods Enzymol. 17B: 356–360.