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• W2062819748 startingPage "1249" @default.
• W2062819748 abstract "Trypsin (Tr) and chymotrypsin (Ch) have similar tertiary structures, yet Tr cleaves peptides at arginine and lysine residues and Ch prefers large hydrophobic residues. Although replacement of the S1 binding site of Tr with the analogous residues of Ch is sufficient to transfer Ch specificity for ester hydrolysis, specificity for amide hydrolysis is not transferred. Trypsin is converted to a Ch-like protease when the binding pocket alterations are further modified by exchange of the Ch surface loops 185 through 188 and 221 through 225 for the analogous Tr loops. These loops are not structural components of either the S1 binding site or the extended substrate binding sites. This mutant enzyme is equivalent to Ch in its catalytic rate, but its substrate binding is impaired. Like Ch, this mutant utilizes extended substrate binding to accelerate catalysis, and substrate discrimination occurs during the acylation step rather than in substrate binding." @default.
• W2062819748 created "2016-06-24" @default.
• W2062819748 creator A5036382303 @default.
• W2062819748 creator A5041318802 @default.
• W2062819748 creator A5083404534 @default.
• W2062819748 date "1992-03-06" @default.
• W2062819748 modified "2023-10-15" @default.
• W2062819748 title "Converting Trypsin to Chymotrypsin: The Role of Surface Loops" @default.
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• W2062819748 doi "https://doi.org/10.1126/science.1546324" @default.
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