Abstract
The intense interest in the metabolic fate of epoxidized xeno-biotics is due to several factors. For instance, epoxides are often intermediates in the lipophile to hydrophile conversions necessary for the excretion of olefinic and aromatic compounds by living systems1, and are widely encountered in man's diet from both natural and man-made sources. Some of these epoxidized compounds may alkylate proteins and nucleic acids and thus include some of the most potent cytotoxins, mutagens and carcinogens known2. In mammals, epoxides may rearrange, deoxygenate to olefins, react with glutathione to form conjugates, or be hydrolysed by water to yield 1,2-diols with or without enzymatic catalysis1,3,4,. The enzymes which catalyse the formation of diols are known as epoxide hydrolases (EC 3.3.2.3), and their subcellular distribution is the subject of this report. Early data showed that styrene oxide hydrolase activity was associated with the microsomal subcellular fraction 5. Epoxide hydrolase activity was subsequently demonstrated on the nuclear6, Golgi apparatus and plasma membranes7, and in the cytosol of the cell8,9, leaving the mitochondria as the last major cellular organelle assumed to be devoid of epoxide hydrolase activity. We now report strong evidence for the occurrence of substantial epoxide hydrolase activity in the mitochondria.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 167-168 |
| Number of pages | 2 |
| Journal | Nature |
| Volume | 291 |
| Issue number | 5811 |
| DOIs | |
| State | Published - 1981 |
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Epoxide hydrolase activity in the mitochondrial fraction of mouse liver. / Gill, Sarjeet S.; Hammock, Bruce D.
In: Nature, Vol. 291, No. 5811, 1981, p. 167-168.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Epoxide hydrolase activity in the mitochondrial fraction of mouse liver
AU - Gill, Sarjeet S.
AU - Hammock, Bruce D.
PY - 1981
Y1 - 1981
N2 - The intense interest in the metabolic fate of epoxidized xeno-biotics is due to several factors. For instance, epoxides are often intermediates in the lipophile to hydrophile conversions necessary for the excretion of olefinic and aromatic compounds by living systems1, and are widely encountered in man's diet from both natural and man-made sources. Some of these epoxidized compounds may alkylate proteins and nucleic acids and thus include some of the most potent cytotoxins, mutagens and carcinogens known2. In mammals, epoxides may rearrange, deoxygenate to olefins, react with glutathione to form conjugates, or be hydrolysed by water to yield 1,2-diols with or without enzymatic catalysis1,3,4,. The enzymes which catalyse the formation of diols are known as epoxide hydrolases (EC 3.3.2.3), and their subcellular distribution is the subject of this report. Early data showed that styrene oxide hydrolase activity was associated with the microsomal subcellular fraction 5. Epoxide hydrolase activity was subsequently demonstrated on the nuclear6, Golgi apparatus and plasma membranes7, and in the cytosol of the cell8,9, leaving the mitochondria as the last major cellular organelle assumed to be devoid of epoxide hydrolase activity. We now report strong evidence for the occurrence of substantial epoxide hydrolase activity in the mitochondria.
AB - The intense interest in the metabolic fate of epoxidized xeno-biotics is due to several factors. For instance, epoxides are often intermediates in the lipophile to hydrophile conversions necessary for the excretion of olefinic and aromatic compounds by living systems1, and are widely encountered in man's diet from both natural and man-made sources. Some of these epoxidized compounds may alkylate proteins and nucleic acids and thus include some of the most potent cytotoxins, mutagens and carcinogens known2. In mammals, epoxides may rearrange, deoxygenate to olefins, react with glutathione to form conjugates, or be hydrolysed by water to yield 1,2-diols with or without enzymatic catalysis1,3,4,. The enzymes which catalyse the formation of diols are known as epoxide hydrolases (EC 3.3.2.3), and their subcellular distribution is the subject of this report. Early data showed that styrene oxide hydrolase activity was associated with the microsomal subcellular fraction 5. Epoxide hydrolase activity was subsequently demonstrated on the nuclear6, Golgi apparatus and plasma membranes7, and in the cytosol of the cell8,9, leaving the mitochondria as the last major cellular organelle assumed to be devoid of epoxide hydrolase activity. We now report strong evidence for the occurrence of substantial epoxide hydrolase activity in the mitochondria.
UR - http://www.scopus.com/inward/record.url?scp=0019489876&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0019489876&partnerID=8YFLogxK
U2 - 10.1038/291167a0
DO - 10.1038/291167a0
M3 - Article
C2 - 7194967
AN - SCOPUS:0019489876
VL - 291
SP - 167
EP - 168
JO - Nature
JF - Nature
SN - 0028-0836
IS - 5811
ER -