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

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Abstract
The 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-N.alpha.1-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 5-8 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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