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PMID: 1067599 Published · ppublish English Journal Article

Model studies of enzymatic NH2-terminal acetylation of porteins with des-Nalpha1-acetyl-alpha-melanotropin as a substrate.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 73 ·No. 9 ·1976-09-00 ·Pages 3010-4

Granger M, Tesser GI, De Jong WW, Bloemendal H

Abstract

The present study describes the acetylation by an enzyme present in calf lens of a synthetic tridecapeptide [analogous to alpha-melanotropin (alpha-melanocyte stimulating hormone) but lacking the naturally occurring NH2-terminal acetyl group: des-Nalpha1-Ac-alpha-melanotropin]. The reaction is specific for the alpha-amino group of the NH2-terminal amino acid. The minimum length required for the substrate to become acetylated appears to be a sequence of five to eight amino acid residues. Modification of the internal lysine decreases the incorporation of acetate, irrespective of the size of the blocking group.

MeSH Terms
Acetates/metabolism Acetylation Amino Acid Sequence Cell-Free System Lens, Crystalline/metabolism Lysine/metabolism Melanocyte-Stimulating Hormones/analysis,metabolism Peptides/metabolism Serine/metabolism Structure-Activity Relationship
Chemicals
Acetates Peptides Serine Melanocyte-Stimulating Hormones Lysine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Granger M
Tesser G I
De Jong W W
Bloemendal H
References (21)
21 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.73.9.3010
Published
1976-09-00
Pages
3010-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430910
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.73.9.3010 PMC Full Text View journal details
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