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Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active beta-carbonic anhydrase from Mycobacterium tuberculosis, Rv3588c
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
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2009 (English)In: Bioorganic & Medicinal Chemistry Letters, ISSN 0960-894X, E-ISSN 1464-3405, Vol. 19, no 23, 6649-6654 p.Article in journal (Refereed) Published
Abstract [en]

The Rv3588c gene product of Mycobacterium tuberculosis, a beta-carbonic anhydrase (CA, EC denominated here mtCA 2, shows the highest catalytic activity for CO2 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.

Place, publisher, year, edition, pages
2009. Vol. 19, no 23, 6649-6654 p.
Keyword [en]
Carbonic anhydrase, Mycobacterium tuberculosis, Rv3588c, Sulfonamide, Enzyme inhibitor
National Category
Biological Sciences
URN: urn:nbn:se:uu:diva-127438DOI: 10.1016/j.bmcl.2009.10.009ISI: 000271430400034PubMedID: 19846301OAI: oai:DiVA.org:uu-127438DiVA: diva2:330052
Available from: 2010-07-14 Created: 2010-07-13 Last updated: 2015-03-31Bibliographically approved

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Mowbray, S.L.
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