Linked Life Data

18242985

Source:http://linkedlifedata.com/resource/pubmed/id/18242985

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2008-3-10
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1464-3405
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1583-7
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Carbonic anhydrase inhibitors: interactions of phenols with the 12 catalytically active mammalian isoforms (CA I-XIV).
pubmed:affiliation
Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't