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Investigation of Potential Inhibitors of Chorismate-Utilizing Enzymes

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11160%2F15%3A10312614" target="_blank" >RIV/00216208:11160/15:10312614 - isvavai.cz</a>

  • Result on the web

    <a href="http://benthamscience.com/journals/current-medicinal-chemistry/volume/22/issue/11/page/1383/" target="_blank" >http://benthamscience.com/journals/current-medicinal-chemistry/volume/22/issue/11/page/1383/</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.2174/0929867322666150209152446" target="_blank" >10.2174/0929867322666150209152446</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Investigation of Potential Inhibitors of Chorismate-Utilizing Enzymes

  • Original language description

    Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria. The absence of these enzymes in humans and their importance in the virulence and survival of bacteria make them suitable targets for potential antimicrobial compounds. Furthermore, the CUE have significant structural homology and similar catalytic mechanisms, enabling the strategy of affecting multiple enzymes with one single inhibitor. This review follows up the investigation of mechanisms of CUE-catalysed reactions and the concurrent development of CUE inhibitors. Many active compounds were found amongst the structures mimicking the transition state of chorismate during the reaction. Most recently, high nanomolar and low micromolar inhibitors against isochorismate-pyruvate lyase were identi

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    FR - Pharmacology and apothecary chemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Current Medicinal Chemistry

  • ISSN

    0929-8673

  • e-ISSN

  • Volume of the periodical

    22

  • Issue of the periodical within the volume

    11

  • Country of publishing house

    AE - UNITED ARAB EMIRATES

  • Number of pages

    17

  • Pages from-to

    1383-1399

  • UT code for WoS article

    000351863400007

  • EID of the result in the Scopus database

    2-s2.0-84925632057