SPECIFICITY AND MOLECULAR PROPERTIES OF PENICILLOLYSIN, A METALLOPROTEINASE FROM PENICILLUM CITRINUM

Article abstract of DOI:10.1016/0031-9422(93)85082-3

The specificity and mode of action of penicillolysin, a metalloproteinase from Penicillum citrinum, were investigated with several bioactive-oligopeptides.The enzyme showed a high affinity toward the Pro-X (X = Gln, Lys, Leu or Arg) bonds of substance P, dynorphin A (1-13), neurotensin and chicken brain pentapeptide, and the R-R bonds in dynorphin A and neurotensin.Preferential cleavages of bonds by the enzyme with hydrophobic amino acid residues at the P₁ position were observed on the peptides used.The specificity of penicillolysin differs from that of other metallopropteinases.The M_r and pI were determined as 18000 and 9.6, respectively.The first 50 amino acids in the N-terminal region were TKETCSNASRKSALEKALSNTVKLANAAATAARSGSASKFSEYEKTTSSS.CD spectra on the hollo- and apo-enzymes of penicillolysin were studied.