Characterization of pyrethroid hydrolysis by the human liver carboxylesterases hCE-1 and hCE-2

Kosuke Nishi, Huazhang Huang, Shizuo G. Kamita, In Hae Kim, Christophe Morisseau, Bruce D. Hammock

Research output: Contribution to journalArticle

85 Scopus citations

Abstract

Carboxylesterases hydrolyze a large array of endogenous and exogenous ester-containing compounds, including pyrethroid insecticides. Herein, we report the specific activities and kinetic parameters of human carboxylesterase (hCE)-1 and hCE-2 using authentic pyrethroids and pyrethroid-like, fluorescent surrogates. Both hCE-1 and hCE-2 hydrolyzed type I and II pyrethroids with strong stereoselectivity. For example, the trans-isomers of permethrin and cypermethrin were hydrolyzed much faster than corresponding cis-counterparts by both enzymes. Kinetic values of hCE-1 and hCE-2 were determined using cypermethrin and 11 stereoisomers of the pyrethroid-like, fluorescent surrogates. Km values for the authentic pyrethroids and fluorescent surrogates were in general lower than those for other ester-containing substrates of hCEs. The pyrethroid-like, fluorescent surrogates were hydrolyzed at rates similar to the authentic pyrethroids by both enzymes, suggesting the potential of these compounds as tools for high throughput screening of esterases that hydrolyze pyrethroids.

Original languageEnglish (US)
Pages (from-to)115-123
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume445
Issue number1
DOIs
StatePublished - Jan 1 2006

Keywords

  • Carboxylesterase
  • Fluorescent substrate
  • Pyrethroid

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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