Overexpression and characterization of a prolyl endopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus

The maltose-regulated mlr-2 gene from the hyperthermophilic archaeon Pyrococcus furiosus was cloned and overexpressed in Escherichia coli. The mlr-2 gene has homology to bacterial and eukaryal prolyl endopeptidase (PEPase). The mlr-2 gene was renamed prpA and its product was purified and characterized. Findings indicated that PrpA has PEPase enzymatic activity. The maltose-dependent regulation of PEPase in P. furiosus was studied and revealed that enzyme activity varies in the same way as prpA mRNA.