The specificity of the S1 and S2 subsites of elastase.
Esters of tetrapeptides of the general formula ethoxycarbonyl-prolyl-alanyl-X-Y where either X or Y was an alanine residue were synthesised and their cleavage by elastase studied. It was found that variation of the alcohol moiety between methyl, cyclohexyl and nitrophenyl residues had no effect on the catalytic rate constant for cleavage of ethoxycarbonyl-prolyl-dialanyl-alanine esters demonstrating that acylation is much faster than deacylation for this system and also that non-productive binding is not kinetically significant. The effect of changing the amino acid residue in position X was small compared with that of change in position Y. The presence of valine and serine residues in position Y produced the highest specificity constant but the highest catalytic rate constant was found for a leucine residue in this position. The results are discussed in terms of the binding of the substrate to the enzyme.
D001665:Binding Sites; D007700:Kinetics; D008433:Mathematics; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism*; D010196:Pancreatic Elastase / Q000378:metabolism*; D013379:Substrate Specificity
D009842:Oligopeptides; D010196:Pancreatic Elastase