Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2010-10-11
pubmed:abstractText
Carbonic anhydrases (CAs, EC 4.2.1.1) belonging to ?-, ?-, ?- and ?-classes and from various organisms, ranging from the bacteria, archaea to eukarya domains, were investigated for their esterase/phosphatase activity with 4-nitrophenyl acetate, 4-nitrophenyl phosphate and paraoxon as substrates. Only ?-CAs showed esterase/phosphatase activity, whereas enzymes belonging to the ?-, ?- and ?-classes were completely devoid of such activity. Paraoxon, the metabolite of the organophosphorus insecticide parathione, was a much better substrate for several human/murine ?-CA isoforms (CA I, II and XIII), with k(cat)/K(M) in the range of 2681.6-4474.9M(-1)s(-1), compared to 4-nitrophenyl phosphate (k(cat)/K(M) of 14.9-1374.4M(-1)s(-1)).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1464-3405
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6208-12
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Paraoxon, 4-nitrophenyl phosphate and acetate are substrates of ?- but not of ?-, ?- and ?-carbonic anhydrases.
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