Abstract
Under ordinary conditions the equilibrium point in protease-catalyzed reactions is near to complete hydrolysis. Therefore, proteases are commonly known for their proteolytic rather than for their proteosynthetic activities. Nevertheless, the proteases have proved to be excellent catalysts in preparative peptide synthetic chemistry. A brief review is given of the historical development of protease-catalyzed peptide synthesis. The theoretical aspects of peptide bond formation are described and particular emphasis is given to techniques for favoring the synthesis of the desired peptide linkages. The applicability of these techniques is exemplified with selected syntheses and semisyntheses. The advantages as well as the problems associated with the enzymatic method are evaluated. A critical assessment is given of the present state of the art and the perspectives of the enzymatic approach to peptide synthetic chemistry.
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01 October 1985
An Erratum to this paper has been published: https://doi.org/10.1007/BF01025499
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Kullmann, W. Proteases as catalytic agents in peptide synthetic chemistry: Shifting the extent of peptide bond synthesis from a “quantité négligeable” to a “quantité considérable”. J Protein Chem 4, 1–22 (1985). https://doi.org/10.1007/BF01025491
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DOI: https://doi.org/10.1007/BF01025491