Substrate-product analogue inhibitors of isoleucine 2-epimerase from Lactobacillus buchneri by rational design
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology
2. Dalhousie University
3. Halifax
4. Canada
5. Department of Chemistry
Abstract
Substrate-product analogues, designed based on partial movement of the sec-butyl side chain during catalysis, inhibit isoleucine 2-epimerase.
Funder
Natural Sciences and Engineering Research Council of Canada
Publisher
Royal Society of Chemistry (RSC)
Subject
Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2019/OB/C9OB01823A
Reference30 articles.
1. Rational design and synthesis of substrate–product analogue inhibitors of α-methylacyl-coenzyme A racemase from Mycobacterium tuberculosis
2. Potent dialkyl substrate-product analogue inhibitors and inactivators of α-methylacyl-coenzyme A racemase from Mycobacterium tuberculosis by rational design
3. Phenylalanine ammonia-lyase: Mirror-image packing of d- and l-phenylalanine and d- and l-transition state analogs into the active site
4. A new model for protein stereospecificity
5. Perturbing the Hydrophobic Pocket of Mandelate Racemase To Probe Phenyl Motion during Catalysis
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Design and evaluation of substrate–product analog inhibitors for racemases and epimerases utilizing a 1,1-proton transfer mechanism;Methods in Enzymology;2023
2. Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition;Chemical Society Reviews;2021
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