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      A novel colorimetric assay for α-methylacyl-CoA racemase 1A (AMACR; P504S) utilizing the elimination of 2,4-dinitrophenolate

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          Abstract

          A versatile continuous colorimetric assay for AMACR is reported.

          Abstract

          α-Methylacyl-CoA racemase (AMACR; P504S) regulates branched-chain fatty acid degradation, activates Ibuprofen and is a recognised cancer drug target. A novel, facile colorimetric assay was developed based on elimination of 2,4-dinitrophenolate. The assay was used to test 5 known inhibitors, determining IC 50 and K i values, reversibility and characterizing irreversible inhibition.

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          A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays

          J-H Zhang (1999)
          Article 0 comments Cited 359 times – based on 0 reviews     Review now
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            Selectivity of nonsteroidal antiinflammatory drugs as inhibitors of constitutive and inducible cyclooxygenase.

            J A Mitchell, P Akarasereenont, C Thiemermann … (1993)
            Constitutive cyclooxygenase (COX-1; prostaglandin-endoperoxide synthase, EC 1.14.99.1) is present in cells under physiological conditions, whereas COX-2 is induced by some cytokines, mitogens, and endotoxin presumably in pathological conditions, such as inflammation. Therefore, we have assessed the relative inhibitory effects of some nonsteroidal antiinflammatory drugs on the activities of COX-1 (in bovine aortic endothelial cells) and COX-2 (in endotoxin-activated J774.2 macrophages) in intact cells, broken cells, and purified enzyme preparations (COX-1 in sheep seminal vesicles; COX-2 in sheep placenta). Similar potencies of aspirin, indomethacin, and ibuprofen against the broken cell and purified enzyme preparations indicated no influence of species. Aspirin, indomethacin, and ibuprofen were more potent inhibitors of COX-1 than COX-2 in all models used. The relative potencies of aspirin and indomethacin varied only slightly between models, although the IC50 values were different. Ibuprofen was more potent as an inhibitor of COX-2 in intact cells than in either broken cells or purified enzymes. Sodium salicylate was a weak inhibitor of both COX isoforms in intact cells and was inactive against COX in either broken cells or purified enzyme preparations. Diclofenac, BW 755C, acetaminophen, and naproxen were approximately equipotent inhibitors of COX-1 and COX-2 in intact cells. BF 389, an experimental drug currently being tested in humans, was the most potent and most selective inhibitor of COX-2 in intact cells. Thus, there are clear pharmacological differences between the two enzymes. The use of such models of COX-1 and COX-2 activity will lead to the identification of selective inhibitors of COX-2 with presumably less side effects than present therapies. Some inhibitors had higher activity in intact cells than against purified enzymes, suggesting that pure enzyme preparations may not be predictive of therapeutic action.
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              Understanding nature's strategies for enzyme-catalyzed racemization and epimerization.

              Martin E. Tanner (2002)
              Epimerases and racemases are enzymes that catalyze the inversion of stereochemistry in biological molecules. In this article, three distinct examples are used to illustrate the wide range of chemical strategies employed during catalysis, and the diverse set of ancestors from which these enzymes have evolved. Glutamate racemase is an example of an enzyme that operates at an "activated" stereocenter (bearing a relatively acidic proton) and employs a nonstereospecific deprotonation/reprotonation mechanism. UDP-N-Acetylglucosamine 2-epimerase acts at an "unactivated" stereocenter and uses a mechanism involving a nonstereospecific elimination/addition of UDP. L-Ribulose phosphate 4-epimerase also acts at an unactivated stereocenter and uses a nonstereospecific retroaldol/aldol mechanism.
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                Author and article information

                Journal
                Journal ID (publisher-id): CHCOFS
                Title: Chemical Communications
                Abbreviated Title: Chem. Commun.
                Publisher: Royal Society of Chemistry (RSC)
                ISSN (Print): 1359-7345
                ISSN (Electronic): 1364-548X
                Publication date Created: 2017
                Publication date (Electronic): 2017
                Volume: 53
                Issue: 37
                Pages: 5087-5090
                Affiliations
                [1 ]Drug & Target Development
                [2 ]Department of Pharmacy & Pharmacology
                [3 ]University of Bath
                [4 ]Bath BA2 7AY
                [5 ]UK
                [6 ]Department of Chemistry
                Article
                DOI: 10.1039/C7CC00476A
                PubMed ID: 28338138
                SO-VID: 66b66303-2d98-4ec8-88e4-65e5adacbdcc
                Copyright © © 2017
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