[1] KARL MARX UNIV,SEKT BIOWISSENSCH,TALSTR 33,O-7010 LEIPZIG,GERMANY
来源:
EUROPEAN JOURNAL OF BIOCHEMISTRY
|
1991年
/
199卷
/
03期
关键词:
D O I:
10.1111/j.1432-1033.1991.tb16163.x
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
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(k(cat)/K(m)) 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.