These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Carbonic anhydrase inhibitors: interactions of phenols with the 12 catalytically active mammalian isoforms (CA I-XIV).
    Author: Innocenti A, Vullo D, Scozzafava A, Supuran CT.
    Journal: Bioorg Med Chem Lett; 2008 Mar 01; 18(5):1583-7. PubMed ID: 18242985.
    Abstract:
    The inhibition of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) with three phenols was investigated. Phenol was an effective CA I-IV, IX, XII and XIV inhibitor (K(I)s of 2.7-11.5 microM) and a less effective one against the other isoforms, CA VA, VB, VI, VII, and XIII (K(I)s of 208-710 micraoM). 3,5-Difluorophenol was an effective inhibitor of CA III, IV, IX, and XIV (K(I)s of 0.71-10.7 microM) being a weaker one for CA I, II, VA, VB, VI, VII, XII, and XIII (K(I)s of 33.9-163 microM). Clioquinol (5-chloro-7-iodo-8-quinolinol) was the best phenol inhibitor against all isozymes, with inhibition constants in the range of 3.3-16.0 microM. These data prove that the phenol OH moiety can be considered as a new 'zinc-water binding group' for the design of CA inhibitors possessing a different inhibition mechanism as compared to the classical sulfonamide inhibitors that bind the metal ion within the active site cavity.
    [Abstract] [Full Text] [Related] [New Search]