peptide alpha-N-acetyltransferase
Identifiers
EC no.2.3.1.88
CAS no.83452-29-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a peptide alpha-N-acetyltransferase (EC 2.3.1.88) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + peptide Nalpha-acetylpeptide + CoA

Thus, the two substrates of this enzyme are acetyl-CoA and peptide, whereas its two products are Nalpha-acetylpeptide and CoA.

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:peptide Nalpha-acetyltransferase. Other names in common use include beta-endorphin acetyltransferase, peptide acetyltransferase, protein N-terminal acetyltransferase, NAT, Nalpha-acetyltransferase, amino-terminal amino acid-acetylating enzyme, and acetyl-CoA:peptide alpha-N-acetyltransferase.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2OB0 and 2PSW.

References

    • Driessen HP, de Jong WW, Tesser GI, Bloemendal H (1985). "The mechanism of N-terminal acetylation of proteins". CRC Crit. Rev. Biochem. 18 (4): 281–325. doi:10.3109/10409238509086784. PMID 3902358.
    • Glembotski CC (1982). "Characterization of the peptide acetyltransferase activity in bovine and rat intermediate pituitaries responsible for the acetylation of beta-endorphin and alpha-melanotropin". J. Biol. Chem. 257 (17): 10501–9. PMID 6286657.
    • O'Donohue TL (1983). "Identification of endorphin acetyltransferase in rat brain and pituitary gland". J. Biol. Chem. 258 (4): 2163–7. PMID 6296134.
    • Tsunasawa S, Kamitani K, Narita K (February 1980). "Partial purification and properties of the amino-terminal amino acid-acetylating enzyme from hen's oviduct". J. Biochem. 87 (2): 645–50. doi:10.1093/oxfordjournals.jbchem.a132789. PMID 6244269.


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