title: The specificity of chymotrypsin. A statistical analysis of hydrolysis data.
abstract: From the literature we collected all available quantitative data on the chymotrypsin-catalyzed hydrolysis of series of amino acid and peptide substrates. Utilizing this data base, we performed calculations on their quantitative structure/activity relationship (QSAR). The substrates were considered to be composed of fragments; log(kcat/Km) values for the substrates resulted from additive contributions of their fragments. Despite the fact that the kinetic constants in the data base were determined by different authors under various reaction conditions, the data are well described by the simple additivity model. Obviously, the intrinsic specificity of chymotrypsin dominates the influence of varying reaction conditions.
authors.affiliation: Sektion Biowissenschaften der Universität Leipzig, Federal Republic of Germany.
authors.forename: V
authors.initials: V
authors.lastname: Schellenberger
authors.forename: K
authors.initials: K
authors.lastname: Braune
authors.forename: H J
authors.initials: HJ
authors.lastname: Hofmann
authors.forename: H D
authors.initials: HD
authors.lastname: Jakubke
mesh_terms: D000595:Amino Acid Sequence; D002918:Chymotrypsin / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008433:Mathematics; D015233:Models, Statistical; D008969:Molecular Sequence Data; D009842:Oligopeptides; D013379:Substrate Specificity
chemical_list: D009842:Oligopeptides; D002918:Chymotrypsin