THE SPECIFICITY OF TRYPSIN
نویسندگان
چکیده
منابع مشابه
Characterization of the S' Subsite Specificity of Trypsin
The S' subsite specificity of bovine trypsin has been studied by partitioning of o-nitrophenylsu1fenyl-Larginyl-trypsin (formed using o-nitrophenylsulfenyl-L-arginine alkyl esters as acyl donors) between various amino acid-derived nucleophiles and water. The data obtained from spectrophotometric measurements confirmed a preference of trypsin for arginine residues in the Pi-position, which is le...
متن کاملTrypsin specificity increased through substrate-assisted catalysis.
Histidine 57 of the catalytic triad of trypsin was replaced with alanine to determine whether the resulting variant would be capable of substrate-assisted catalysis [Carter, P., & Wells, J. A. (1987) Science 237, 394-9]. A 2.5-fold increase in kcat/Km was observed on tri- or tetrapeptide substrates containing p-nitroanilide leaving groups and histidine at P2. In contrast, hydrolysis of peptide ...
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Recognition for proteolysis by trypsin depends almost exclusively on tight binding of arginine or lysine side chains by the primary substrate specificity pocket. Although extended subsite interactions are important for catalysis, the majority of binding energy is localized in the P1 pocket. Analysis of the interactions of trypsin with the P1 residue of the bound inhibitors ecotin and bovine pan...
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1. The maltase of saliva and that of E. coli (B. coli communis) hydrolyze maltose but not alpha-methylglucoside or sucrose and are therefore to be considered glucomaltases. 2. Maltase is rapidly and completely inactivated and digested by trypsin.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1939
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)73769-1