The Mechanism of N-Terminal Acetylation of Protein

H.P.C. Driessen(Radboud University Nijmegen), W.W. de Jong(Radboud University Nijmegen), G. I. Tesser(Radboud University Nijmegen), H. Bloemendal(Radboud University Nijmegen)
Critical Reviews in Biochemistry
January 1, 1985
Cited by 237

Abstract

N alpha-acetylation is almost exclusively restricted to eukaryotic structural proteins. As a rule it is a post-initiational process, requiring the presence of the enzyme N alpha-acetyltransferase and the acetyl donor acetylcoenzyme A. N alpha-acetyltransferases appear to have a narrow substrate specificity, which is very similar for enzymes from different tissues and species. Amino acids predominantly present at the N terminus of N alpha-acetylated proteins are alanine, serine, and methionine. The occurrence of these residues is apparently a prerequisite for acetylation. The region following these amino acids is also important. If methionine is at the N terminus, the second position is always occupied by a strongly hydrophilic amino acid. Two- and three-dimensional structural characteristics of the protein do not seem to play a major role in N alpha-acetylation. Up to now the exact function for N alpha-acetylation is not known.


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