Serine O-acetyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a serine O-acetyltransferase (EC 2.3.1.30) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + L-serine $\rightleftharpoons$ CoA + O-acetyl-L-serine

Thus, the two substrates of this enzyme are acetyl-CoA and L-serine, whereas its two products are CoA and O-acetyl-L-serine.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:L-serine O-acetyltransferase. Other names in common use include SATase, L-serine acetyltransferase, serine acetyltransferase, and serine transacetylase. This enzyme participates in cysteine metabolism and sulfur metabolism.

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

[edit] Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1S80, 1SSM, 1SSQ, 1SST, 1T3D, 1Y7L, and 2ISQ.

[edit] References

IUBMB entry for 2.3.1.30
BRENDA references for 2.3.1.30 (Recommended.)
PubMed references for 2.3.1.30
PubMed Central references for 2.3.1.30
Google Scholar references for 2.3.1.30
Kredich NM, Tomkins GM (1966). "The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium". J. Biol. Chem. 241: 4955–65. PMID 5332668.
Smith IK, Thompson JF (1971). "Purification and characterization of L-serine transacetylase and O-acetyl-L-serine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris)". Biochim. Biophys. Acta. 227: 288–95. PMID 5550822.