Oligopeptidase B (opdB, EC is a member of the prolyl oligopeptidase family of serine peptidases and unrelated to the trypsin and subtilisin families. It is a potential processing enzyme of prokaryotes to produce biologically active products, being very specific for the basic amino acid pairs of polypeptides. Bacterial oligopeptidase B cleaves globular proteins, albeit in a highly restricted fashion. While most members of this peptidase family hydrolyse peptide bonds at the C-terminal side of proline residues, oligopeptidase B exhibits a trypsin-like substrate specificity, cleaving peptides after basic residues (arginine or lysine). Oligopeptidase B was first cloned and characterized from , and has also been described in other prokaryotes. Similar enzymes have been found in plants and some other higher organisms. We report the isolation of two different new oligopeptidase B bacterial strains producers. We identified the two genes, designated opdB1 and opB. The opdB genes encodes a 703-residue peptide with high homology to the oligopeptidase B family in prokaryotes. The isolated opdB gave the highest similarity score to oligopeptidase B of strain K279a (GenBank ). To reveal the structural and kinetic properties of oligopeptidase B in more detail, we have cloned, expressed, and purified the enzymes to produce sufficient material to help in physical investigations, including NMR and x-ray crystallographic measurements. We also carried out a molecular characterization study of the two enzymes.


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  1. F.B. Rashidi, H. El Shanti, S. Goda, Screening for and cloning and molecular characterization of two new oligopeptidase B encoding genes, QFARF Proceedings, 2010, BMP4.
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