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Research article2009Peer reviewed

Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active beta-carbonic anhydrase from Mycobacterium tuberculosis, Rv3588c

Carta, F; Maresca, A; Suarez Covarrubias, A; Mowbray, Sherry; Jones, TA; Supuran, CT


The Rv3588c gene product of Mycobacterium tuberculosis, a beta-carbonic anhydrase (CA, EC denominated here mtCA 2, shows the highest catalytic activity for CO(2) hydration (k(cat) of 9.8 x 10(5) s(-1), and k(cat)/K(m) of 9.3 x 10(7) M(1) s(1)) among the three beta-CAs encoded in the genome of this pathogen. A series of sulfonamides/sulfamates was assayed for their interaction with mtCA 2, and some diazenylbenzenesulfonamides were synthesized from sulfanilamide/metanilamide by diazotization followed by coupling with amines or phenols. Several low nanomolar mtCA 2 inhibitors have been detected among which acetazolamide, ethoxzolamide and some 4-diazenylbenzenesulfonamides (K(I)s of 9-59 nM). As the Rv3588c gene was shown to be essential to the growth of M. tuberculosis, inhibition of this enzyme may be relevant for the design of antituberculosis drugs possessing a novel mechanism of action. (C) 2009 Elsevier Ltd. All rights reserved.


Carbonic anhydrase; Mycobacterium tuberculosis; Rv3588c; Sulfonamide; Enzyme inhibitor

Published in

Bioorganic and Medicinal Chemistry Letters
2009, Volume: 19, number: 23, pages: 6649-6654

      SLU Authors

    • Mowbray, Sherry

      • Department of Molecular Biology, Swedish University of Agricultural Sciences

    Sustainable Development Goals

    SDG3 Good health and well-being

    UKÄ Subject classification

    Organic Chemistry

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