SPECIFICITY AND MOLECULAR-PROPERTIES OF PENICILLOLYSIN, A METALLOPROTEINASE FROM PENICILLIUM-CITRINUM

The specificity and mode of action of penicillolysin, a metalloprotein ase from Penicillium citrinum, were investigated with several bioactiv e-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), neu rotensin and chicken brain pentapeptide, and the R-R bonds in dynorphi n A and neurotensin. Preferential cleavages of bonds by the enzyme wit h hydrophobic amino acid residues at the P1 position were observed on the peptides used. The specificity of penicillolysin differs from that of other metalloproteinases. The M(r) and pI were determined as 18 00 0 and 9.6, respectively. The first 50 amino acids in the N-terminal re gion were KETCSNASkKSALEKALSNTVKLANAAATAARSGSASKFSEYEKTTSSS. CD spectr a on the hollo- and apo-enzymes of penicillolysin were studied.