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

Disciplines

Medicine and Health Sciences

PubMedID

3756175

Department(s)

Department of Medicine

Document Type

Article

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