A study on the AMACR catalysed elimination reaction and its application to inhibitor testing
Author:
Affiliation:
1. Medicinal Chemistry
2. Department of Pharmacy & Pharmacology
3. University of Bath
4. Bath BA2 7AY
5. UK
6. Department of Chemistry
Abstract
The elimination of fluoride from 3-fluoro-2-methylacyl-CoA substrates by α-methylacyl-CoA racemase (AMACR 1A; P504S) was investigated as a method for determining enzyme activity and inhibitor potency.
Funder
University of Bath
Prostate Cancer UK
Publisher
Royal Society of Chemistry (RSC)
Subject
Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2016/OB/C5OB01541C
Reference57 articles.
1. Purification and Characterization of an alpha-Methylacyl-CoA Racemase from Human Liver
2. Purification and properties of an alpha-methylacyl-CoA racemase from rat liver
3. α-Methylacyl-CoA racemase (AMACR): Metabolic enzyme, drug metabolizer and cancer marker P504S
4. Synthesis and use of isotope-labelled substrates for a mechanistic study on human α-methylacyl-CoA racemase 1A (AMACR; P504S)
5. Chiral inversion of 2-arylpropionyl-CoA esters by human α-methylacyl-CoA racemase 1A (P504S)—a potential mechanism for the anti-cancer effects of ibuprofen
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1. Analysis of enzyme reactions using NMR techniques: A case study with α-methylacyl-CoA racemase (AMACR);Methods in Enzymology;2023
2. Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition;Chemical Society Reviews;2021
3. Carbon–fluorine bond cleavage mediated by metalloenzymes;Chemical Society Reviews;2020
4. Novel 2-arylthiopropanoyl-CoA inhibitors of α-methylacyl-CoA racemase 1A (AMACR; P504S) as potential anti-prostate cancer agents;Bioorganic Chemistry;2019-11
5. Identification of novel small-molecule inhibitors of α-methylacyl-CoA racemase (AMACR; P504S) and structure-activity relationships;Bioorganic Chemistry;2019-11
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