Active-site-directed inactivation of human liver alpha-L-fucosidase by conduritol C trans-epoxide.
Publication/Presentation Date
9-26-1986
Abstract
Conduritol C trans-epoxide was found to inactivate human liver alpha-L-fucosidase (alpha-L-fucoside fucohydrolase, EC 3.2.1.51), exhibiting an apparent dissociation constant of 43 mM. The cis-isomer of the inactivator had no apparent effect on the enzyme's activity. The pH profile for the inactivation yielded two apparent pK values of approx. 3.7 and 6.1 alpha-L-Fucose (a competitive inhibitor) was effective in protecting the enzyme from inactivation. These results are consistent with a requirement for two amino acid side chains at the active site involved in the reaction of the enzyme with conduritol C trans-epoxide.
Volume
873
Issue
2
First Page
198
Last Page
203
ISSN
0006-3002
Published In/Presented At
White, W. J., Jr, Schray, K. J., Legler, G., & Alhadeff, J. A. (1986). Active-site-directed inactivation of human liver alpha-L-fucosidase by conduritol C trans-epoxide. Biochimica et biophysica acta, 873(2), 198–203. https://doi.org/10.1016/0167-4838(86)90046-4
Disciplines
Medicine and Health Sciences
PubMedID
3756175
Department(s)
Department of Medicine
Document Type
Article