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PMID: 3902358 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

The mechanism of N-terminal acetylation of proteins.

CRC critical reviews in biochemistry ·Vol. 18 ·No. 4 ·1985-00-00 ·Pages 281-325

Driessen HP, de Jong WW, Tesser GI, Bloemendal H

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.

MeSH Terms
Acetylation Acetyltransferases/metabolism Amino Acid Sequence Amino Acids/analysis Animals Genes Humans Kinetics Protein Processing, Post-Translational Proteins/genetics,metabolism Rats Structure-Activity Relationship Tissue Distribution
Chemicals
Amino Acids Proteins Acetyltransferases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Driessen H P
de Jong W W
Tesser G I
Bloemendal H
Article Info
Journal
CRC critical reviews in biochemistry
Abbr.
CRC Crit Rev Biochem
ISSN
0045-6411
Published
1985-00-00
Pages
281-325
Language
English
Region
United States
NLM ID
0330403
Subset
IM
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