Open AccessModel studies of enzymatic NH2-terminal acetylation of porteins with des-Nalpha1-acetyl-alpha-melanotropin as a substrate.
Author(s) -
Michèle Granger,
G. I. Tesser,
W.W. de Jong,
H. Bloemendal
Publication year - 1976
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.73.9.3010
Subject(s) - acetylation , enzyme , lysine , alpha (finance) , biochemistry , substrate (aquarium) , stereochemistry , amino acid , chemistry , peptide sequence , biology , medicine , ecology , gene , nursing , construct validity , patient satisfaction
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.
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