Phytochemistry p. 1317 - 1322 (1993)
Update date:2022-08-03
Topics:
Yamaguchi, Megumi
Hanzawa, Satoshi
Hirano, Ken-Ichi
Yamagata, Youhei
Ichishima, Eiji
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 Mr 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.
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