MOLECULAR-CLONING OF CDNA FOR SARCOPHAGA PROLYL ENDOPEPTIDASE AND CHARACTERIZATION OF THE RECOMBINANT ENZYME PRODUCED BY AN ESCHERICHIA-COLI EXPRESSION SYSTEM

A cDNA for prolyl endopeptidase (PEP) of Sarcophaga peregrina (flesh f ly) was cloned and its sequence determined. The overall amino acid seq uence identity between Sarcophaga and mammalian PEPs was 53%, indicati ng that these enzymes are structurally very similar. Northern blot hyb ridization revealed that the Sarcophaga PEP gene was activated signifi cantly at the eversion stage of imaginal disc differentiation. We obta ined recombinant PEP by expressing the cDNA in Escherichia coli. The r ecombinant and authentic enzymes showed almost identical characteristi cs, in terms of substrate specificities and sensitivities to inhibitor s. (C) 1997 Elsevier Science Ltd.