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Unusual specificity of polyethylene glycol-modified thermolysin in peptide synthesis catalyzed in organic solvents

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Summary

Polyethylene glycol-modified thermolysin was found to efficiently catalyze peptide synthesis in organic solvents. As in aqueous media, the reaction occurred through a rapid equilibrium random bireactant mechanism. However, the substrate specificity of modified thermolysin was actually changed since hydrophilic as well as acidic amino acids were better carboxyl group donors than hydrophobic residues, contrary to what is observed in both the enzyme-catalyzed synthesis and hydrolysis of peptide bonds in water.

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Authors and Affiliations

  1. Centre de Biochimie et de Biologie Moléculaire du CNRS, BP 71, 13402, Marseille Cedex 9, France

    Anne Ferjancic, Antoine Puigserver & Hubert Gaertner

Authors
  1. Anne Ferjancic
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  2. Antoine Puigserver
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  3. Hubert Gaertner
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Ferjancic, A., Puigserver, A. & Gaertner, H. Unusual specificity of polyethylene glycol-modified thermolysin in peptide synthesis catalyzed in organic solvents. Biotechnol Lett 10, 101–106 (1988). https://doi.org/10.1007/BF01024634

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