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 language | English (US) |
|---|---|
| Pages (from-to) | 115-123 |
| Number of pages | 9 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 445 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 2006 |
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Keywords
- Carboxylesterase
- Fluorescent substrate
- Pyrethroid
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Characterization of pyrethroid hydrolysis by the human liver carboxylesterases hCE-1 and hCE-2. / Nishi, Kosuke; Huang, Huazhang; Kamita, Shizuo G.; Kim, In Hae; Morisseau, Christophe; Hammock, Bruce D.
In: Archives of Biochemistry and Biophysics, Vol. 445, No. 1, 01.01.2006, p. 115-123.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of pyrethroid hydrolysis by the human liver carboxylesterases hCE-1 and hCE-2
AU - Nishi, Kosuke
AU - Huang, Huazhang
AU - Kamita, Shizuo G.
AU - Kim, In Hae
AU - Morisseau, Christophe
AU - Hammock, Bruce D.
PY - 2006/1/1
Y1 - 2006/1/1
N2 - 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.
AB - 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.
KW - Carboxylesterase
KW - Fluorescent substrate
KW - Pyrethroid
UR - http://www.scopus.com/inward/record.url?scp=29244491449&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=29244491449&partnerID=8YFLogxK
U2 - 10.1016/j.abb.2005.11.005
DO - 10.1016/j.abb.2005.11.005
M3 - Article
VL - 445
SP - 115
EP - 123
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1
ER -