The structure-activity relationship of the papain hydrolysis of N-benzoylglycine esters.
The relationship between structure and the Michaelis-Menten constants (Km) for the papain hydrolysis of a series of 37 N-benzoylglycine esters was investigated. The series studied comprises a wide range of aromatic and aliphatic esters with a 5000-fold variation in their Km constants and essentially constant kcat values. It was found that the variation in the Km constants could be rationalized by the following quantitative structure-activity relationship (QSAR): log 1/Km = 8.13F + 0.33Z + 1.27II3' + 1.95. In this equation F is the field inductive parameter, II3' is the hydrophobic constant for the more lipophilic of the two possible meta substituents and Z is the Van der Waals distance from oxygen through the end of the molecule, in the direction of the 4 position of the aromatic ester moiety.
Compadre
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CM
Department of Chemistry, Pomona College, Claremont, CA 91711.
Hansch
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C
Klein
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Langridge
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R
D003198:Computer Simulation; D005998:Glycine / Q000031:analogs & derivatives* / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D010206:Papain / Q000378:metabolism*; D013329:Structure-Activity Relationship
D010206:Papain; D005998:Glycine