QM/MM Study of the Catalytic Reaction of Myrosinase; Importance of Assigning Proper Protonation States of Active-Site Residues
Author:
Affiliation:
1. Department of Chemistry, University of Kurdistan, 66175-416 Sanandaj, Iran
2. Department of Theoretical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden
Funder
Vetenskapsr?det
University of Kurdistan
Publisher
American Chemical Society (ACS)
Subject
Physical and Theoretical Chemistry,Computer Science Applications
Link
http://pubs.acs.org/doi/pdf/10.1021/acs.jctc.0c01121
Reference98 articles.
1. Glucosinolates and their breakdown products in food and food plants
2. The crystal structures of Sinapis alba myrosinase and a covalent glycosyl–enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase
3. Chemical and biological properties of indole glucosinolates (glucobrassicins): A review
4. High resolution refinement of β‐galactosidase in a new crystal form reveals multiple metal‐binding sites and provides a structural basis for α‐complementation
5. On expanding the repertoire of glycosynthases: Mutant β-galactosidases forming β-(1,6)-linkages
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