Soo Suk Lee, Zhi-hong Li, Dong Ha Lee
1995
Citations
0
Influential Citations
14
Citations
Journal
Journal of The Chemical Society-perkin Transactions 1
Abstract
2-Benzyl-3,4-epoxybutanoic acid (BEBA) was studied as an irreversible inhibitor for the zinc-containing protease, carboxypeptidase A. Of four possible stereoisomers, those having a 2R, 3S- and a 2S, 3R-configuration inhibited carboxypeptidase A in a time-dependent manner. The latter compound that belongs to the D series is more effective with a kinact/Ki value of 139.5 dm3 mol–1 s–1 than the former having a Kinact/Ki value of 53.9 dm3 mol–1 s–1. Partition ratios for (2R, 3S)- and (2S, 3R)-BEBA were determined as 1.01 and 0.53, respectively. The observed kinetic parameters reveal that both are highly efficient and fast acting pseudomechanism-based inactivators for carboxypeptidase A. Details of the kinetic analyses, design principles and asymmetric syntheses of these inactivators are described.