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-Reference-Cited by-同舟云学术

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

Published:1991-06 Issue:18 Volume:266 Page:11628-11631
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Høj P.B.,Rodriguez E.B.,Iser J.R.,Stick R.V.,Stone B.A.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. [25] Application of affinity labeling for studying structure and function of enzymes

2. 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

3. Affinity labeling of creatine kinase by N-(2,3-epoxypropyl)-N-amidinoglycine.

4. Specific and Irreversible Inactivation of Pepsin by Substrate-like Epoxides

5. Isolation and Amino Acid Sequence of a Peptide Containing an Epoxide-Reactive Residue from the Thermolysin-Digest of Scytalidium lignicolum Acid Protease B1

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