Kinetic-Studies on Cyclophellitol Analogs - Mechanism-Based Inactivators

V. W.F. Tai, P. H. Fung, Y. S. Wong, T. K.M. Shing

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


The (1R,6S)- and (1R,2S,6S)-diastereoisomers of cyclophellitol were found to be effective irreversible inactivators of α-D-glucosidase and α-D-mannosidase, respectively. The (1R,6S)-diastereoisomer inactivates brewers yeast α-D-glucosidase according to pseudo-first order kinetics with inactivation constants of Ki = 26.9 μM, ki = 0.401 min-1 while the (1R,2S,6S)-diastereoisomer inactivates jack beans α-D-mannosidase in a similar manner with Ki = 120 μM, ki = 2.85 min-1. The irreversibility of these compounds was evidenced by the lack of reactivation upon dialysis of the inactivated enzyme.

Original languageEnglish
Pages (from-to)175-180
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 1995 Aug 1

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Kinetic-Studies on Cyclophellitol Analogs - Mechanism-Based Inactivators'. Together they form a unique fingerprint.

Cite this