PMID: 3756175Sep 26, 1986Paper

Active-site-directed inactivation of human liver alpha-L-fucosidase by conduritol C trans-epoxide

Biochimica Et Biophysica Acta
W J WhiteJ A Alhadeff

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.

References

Jun 9, 1978·Biochimica Et Biophysica Acta·T Alam, A S Balsubramanian
Jan 1, 1979·Methods in Enzymology·W W Cleland
Jul 1, 1985·Biochimica Et Biophysica Acta·W J WhiteJ A Alhadeff
Dec 15, 1981·Biochimica Et Biophysica Acta·D S Grove, G S Serif

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Citations

Jan 1, 1991·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·S W Johnson, J A Alhadeff
Jul 20, 2011·Organic & Biomolecular Chemistry·Martin D WitteHerman S Overkleeft
Mar 18, 1987·Biochimica Et Biophysica Acta·W J WhiteJ A Alhadeff

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