The characterisation of the reaction between (r,s)2′,3′-epoxypropyl β-d-glucopyranoside and yeast hexokinase: Evidence for the presence of a cysteine residue in the binding site of d-glucose
Author:
Publisher
Elsevier BV
Subject
Toxicology,General Medicine
Reference20 articles.
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3. The use of deoxyfluoro-d-glucopyranoses and related compounds in a study of yeast hexokinase specificity;Bessell;Biochem. J.,1972
4. An active site-directedx irreversible Inactivation of yeast hexokinase by (R,S)2′,3′-epoxypropyl β-d-glucopyranoside;Bessell;Chem.-Biol. Interactions,1973
5. (R,S)2′,3′-epoxypropyl ethers and glucosides of d-glucopyranose;Bessell;Carbohydrate Res.,1972
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1. Identification of an essential glutamate residue in the active site of endoglucanase III fromTrichoderma reesei;FEBS Letters;1993-01-25
2. Active site-directed inhibition by optically pure epoxyalkyl cellobiosides reveals differences in active site geometry of two 1,3-1,4-beta-D-glucan 4-glucanohydrolases. The importance of epoxide stereochemistry for enzyme inactivation;Journal of Biological Chemistry;1991-06
3. Differences in Active Site Structure in a Family of β-glucan Endohydrolases Deduced from the Kinetics of Inactivation by Epoxyalkyl β-Oligoglucosides;Journal of Biological Chemistry;1989-03
4. Active-site-directed inactivation of Schizophyllum commune cellulase by 4′, 5′-epoxypentyl-4-D-(β-D-glucopyranosyl)-β-D-glucopyranoside;Biochemistry and Cell Biology;1988-08-01
5. Affinity Labeling of Soybean β-Amylase with 2′,3′-Epoxypropyl α-D-Glucopyranoside;The Journal of Biochemistry;1986
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