Arylamine N-acetyltransferase

From Wikipedia, the free encyclopedia

In enzymology, an arylamine N-acetyltransferase (EC 2.3.1.5) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + an arylamine $\rightleftharpoons$ CoA + an N-acetylarylamine

Thus, the two substrates of this enzyme are acetyl-CoA and arylamine, whereas its two products are CoA and N-acetylarylamine.

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:arylamine N-acetyltransferase. Other names in common use include arylamine acetylase, beta-naphthylamine N-acetyltransferase, 4-aminobiphenyl N-acetyltransferase, acetyl CoA-arylamine N-acetyltransferase, 2-naphthylamine N-acetyltransferase, arylamine acetyltransferase, indoleamine N-acetyltransferase, N-acetyltransferase, p-aminosalicylate N-acetyltransferase, serotonin acetyltransferase, and serotonin N-acetyltransferase.

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 1GX3, 1W5R, 1W6F, 2BSZ, 2IJA, 2PFR, and 2PQT.

[edit] References

IUBMB entry for 2.3.1.5
BRENDA references for 2.3.1.5 (Recommended.)
PubMed references for 2.3.1.5
PubMed Central references for 2.3.1.5
Google Scholar references for 2.3.1.5
CHOU TC, LIPMANN F (1952). "Separation of acetyl transfer enzymes in pigeon liver extract". J. Biol. Chem. 196: 89–103. PMID 12980945.
Paul RC, Ratledge C (1973). "Further studies on anthranilate N-acetyltransferase and the metabolism of N-acetylanthranilic acid in Aerobacter aerogenes". Biochim. Biophys. Acta. 320: 9–15. PMID 4748369.
Tabor H, Mehler AH and Stadtman ER (1953). "The enzymatic acetylation of amines". J. Biol. Chem. 204: 127–138.
Weissbach H, Redfield BG and Axelrod J (1961). "The enzymic acetylation of serotonin and other naturally occurring amines". Biochim. Biophys. Acta 54: 190–192. doi:10.1016/0006-3002(61)90954-4.