Irreversible inhibition of the thermophilic esterase EST2 from Alicyclobacillus acidocaldarius (Articolo in rivista)

Type
Label
  • Irreversible inhibition of the thermophilic esterase EST2 from Alicyclobacillus acidocaldarius (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1007/s00792-008-0179-1 (literal)
Alternative label
  • Febbraio F.; Esposito D'Andrea S.; Mandrich L.; Merone L.; Rossi M.; Nucci R.; Manco G. (2008)
    Irreversible inhibition of the thermophilic esterase EST2 from Alicyclobacillus acidocaldarius
    in Extremophiles (Tokyo, Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Febbraio F.; Esposito D'Andrea S.; Mandrich L.; Merone L.; Rossi M.; Nucci R.; Manco G. (literal)
Pagina inizio
  • 719 (literal)
Pagina fine
  • 728 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 12 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 5 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biochimica delle Proteine, CNR, Via P. Castellino 111, 80131 Naples, Italy (literal)
Titolo
  • Irreversible inhibition of the thermophilic esterase EST2 from Alicyclobacillus acidocaldarius (literal)
Abstract
  • Kinetic studies of irreversible inhibition in recent years have received growing attention owing to their relevance to problems of basic scientific interest as well as to their practical importance. Our studies have been devoted to the characterization of the effects that well-known acetylcholinesterase irreversible inhibitors exert on a carboxylesterase (EST2) from the thermophilic eubacterium Alicyclobacillus acidocaldarius. In particular, sulfonyl inhibitors and the organophosphorous insecticide diethyl-p-nitrophenyl phosphate (paraoxon) have been studied. The incubation of EST2 with sulfonyl inhibitors resulted in a time-dependent inactivation according to a pseudo-first-order kinetics. On the other hand, the EST2 inactivation process elicited by paraoxon, being the inhibition reaction completed immediately after the inhibitor addition, cannot be described as a pseudo-first-order kinetics but is better considered as a high affinity inhibition. The values of apparent rate constants for paraoxon inactivation were determined by monitoring the enzyme/substrate reaction in the presence of the inhibitor, and were compared with those of the sulfonyl inhibitors. The protective effect afforded by a competitive inhibitor on the EST2 irreversible inhibition, and the reactivation of a complex enzyme/irreversible-inhibitor by hydroxylamine and 2-PAM, were also investigated. The data have been discussed in the light of the recently described dual substrate binding mode of EST2, considering that the irreversible inhibitors employed were able to discriminate between the two different binding sites. (literal)
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