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Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate

  1. Author:
    Wlodawer, A.
    Li, M.
    Gustchina, A.
    Oyama, H.
    Oda, K.
    Beyer, B. B.
    Clemente, J.
    Dunn, B. M.

  2. Author Address

    Wlodawer, A, NCI, Prot Struct Sect, Macromol Crystallog Lab, Frederick, MD 21702 USA NCI, Prot Struct Sect, Macromol Crystallog Lab, Frederick, MD 21702 USA. NCI, Intramural Res Support Program, SAIC Frederick, Frederick, MD 21702 USA. Kyoto Inst Technol, Fac Text Sci, Dept Appl Biol, Sakyo Ku, Kyoto 6068585, Japan. Univ Florida, Dept Biochem & Mol Biol, Gainesville, FL 32610 USA.
    1. Year: 2004
  2. Journal: Biochemical and Biophysical Research Communications
    1. 314
    2. 2
    3. Pages: 638-645
  4. Type of Article: Article
  1. Abstract:

    High-resolution crystallographic analysis of a complex of the serine-carboxyl proteinase sedolisin with pseudo-iodotyrostatin revealed two molecules of this inhibitor bound in the active site of the enzyme, marking subsites from S3 to S3'. The mode of binding represents two products of the proteolytic reaction. Substrate specificity of sedolisin was investigated using peptide libraries and a new peptide substrate for sedolisin, MCA-Lys-Pro-Pro-Leu-Glu#Tyr-Arg-Leu-Gly-Lys(DNP)-Gly, was synthesized based on the results of the enzymatic and crystallographic studies and was shown to be efficiently cleaved by the enzyme. The kinetic parameters for the substrate, measured by the increase in fluorescence upon relief of quenching, were: k(cat) = 73 +/- 5 s(-1), K-m = 0.12 +/- 0.011 muM, and k(cat)/K-m = 608 +/- 85 s(-1) muM(-1). Published by Elsevier Inc

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