Purification and Properties of a Periplasmic Aminoendopeptidase from <i>Escherichia coli</i>
European Journal of BiochemistryPublished 1 December 1975Open access
Claude Lazdunski, Jeanine Busuttil, Andrée Lazdunski
Citations66
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TL;DR
A periplasmic aminoendopeptidase from Escherichia coli has been purified to hemogeneity and the study of its substrate specificity indicated that the enzyme has both aminopePTidase and endopeptIDase activity.
Abstract
A periplasmic aminoendopeptidase from Escherichia coli has been purified to hemogeneity. It is a monomer of molecular weight 45000 and containing one -- SH group that is necessary for catalytic activity. The study of its substrate specificity indicated that the enzyme has both aminopeptidase and endopeptidase activity. The pH optimum for L-alanine p-nitroanilide hydrolysis is between 7 and 7.5 and that for 125I-labeled casein proteolysis between 7.3 and 7.6. The activation energy for the hydrolysis of L-anine p-nitroanilide was calculated to be 5.3 kcal X mol-1 (22.2 kJ X mol-1).
Keywords
Agricultural and Biological SciencesMedicineNeuroscience
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