Abstract
Chymosin (EC 3.4.23.4, formerly rennin) is one of the primary enzymes used to initiate milk clotting for cheese production (MacKinlay & Wake, 1971). This process begins with the specific cleavage of the Phe105*Met106 peptide bond of κ-casein by this enzyme (Jolies et al., 1968). The sequence of this cleavage site is
A number of studies with synthetic peptides, which were designed based on the 103–108 κ-casein sequence, have been undertaken to determine the kinetic parameters of chymosin (e.g., Visser & Rollema, 1986), and recently studies by Visser and coworkers (1987) have been performed which provide information concerning the substrate specificity of this enzyme. Based upon the results of these kinetic and model building studies, it was proposed that residues 103–108 fit snugly into the active site cleft and that the addition of the 98–102 sequence, -His-Pro-His-Pro-His-, assisted in the positioning of the 103–108 peptide segment into the active site by its favorable electrostatic interactions with residues on the protein surface.
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© 1991 Plenum Press, New York
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Gilliland, G.L., Oliva, M.T., Dill, J. (1991). Functional Implications of the Three-Dimensional Structure of Bovine Chymosin. In: Dunn, B.M. (eds) Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 306. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6012-4_3
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DOI: https://doi.org/10.1007/978-1-4684-6012-4_3
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