Solov'eva N I, Balaevskaia T O, Finogenova M P, Shibnev V A
Bioorg Khim. 1994 Mar;20(3):303-9.
Interactions of collagenases I and II (clostridiopeptidases) from Clostridium histolyticum with hexapeptide substrates in which some L-proline residues are replaced by their D-analogues, as well as with the tripeptide chloromethyl ketone Z-Gly-Pro-Gly-CH2Cl were studied. A role of stereochemistry of the amino acid residues in the substrate was established and differences between the collagenases, with regard to their specific requirements to substrates, were revealed. The tripeptide chloromethyl ketone is shown to be a specific collagenase inhibitor modifying at the substrate-binding site in the active centre of these enzymes, most likely lysine residues.
研究了溶组织梭菌的胶原酶I和II（梭菌肽酶）与一些L-脯氨酸残基被其D-类似物取代的六肽底物以及三肽氯甲基酮Z-Gly-Pro-Gly-CH₂Cl的相互作用。确定了底物中氨基酸残基立体化学的作用，并揭示了这两种胶原酶在对底物的特定要求方面的差异。三肽氯甲基酮被证明是一种特异性胶原酶抑制剂，它在这些酶活性中心的底物结合位点进行修饰，最有可能修饰的是赖氨酸残基。
