Enzymic cleavage of the blocked amino terminal residues of peptides.
The substrate specificity of an enzyme that removes some N-terminal blocked amino acids from blocked peptides has been further explored with several naturally-occurring peptides. Chloride ion is an effective modulator of enzyme activity. Although the relative efficiency of the enzyme varies considerably with different peptide substrates, in each case there was significant although less than quantitative release of the N-terminal blocked amino acid. The possible application of this enzyme to structural studies on polypeptides is evaluated.
D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases / Q000032:analysis / Q000378:metabolism*; D002712:Chlorides / Q000494:pharmacology; D010455:Peptides / Q000032:analysis*; D013379:Substrate Specificity
D000596:Amino Acids; D002712:Chlorides; D010455:Peptides; D000626:Aminopeptidases