Epoxide hydrolase activity in the mitochondrial fraction of mouse liver

Sarjeet S. Gill, Bruce D. Hammock

Research output: Contribution to journalArticle

30 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)167-168
Number of pages2
JournalNature
Volume291
Issue number5811
DOIs
StatePublished - 1981

Fingerprint

Epoxide Hydrolases
Liver
Epoxy Compounds
mouse EPHX1 protein
Mitochondria
Subcellular Fractions
Cytotoxins
Mutagens
Alkenes
Golgi Apparatus
Organelles
Carcinogens
Cytosol
Nucleic Acids
Glutathione
Mammals
Diet
Water
Enzymes
Proteins

ASJC Scopus subject areas

  • General

Cite this

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 journalArticle

Gill, Sarjeet S. ; Hammock, Bruce D. / Epoxide hydrolase activity in the mitochondrial fraction of mouse liver. In: Nature. 1981 ; Vol. 291, No. 5811. pp. 167-168.
@article{e449e841b8f64cab9656c8dcc100b6b7,
title = "Epoxide hydrolase activity in the mitochondrial fraction of mouse liver",
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.",
author = "Gill, {Sarjeet S.} and Hammock, {Bruce D.}",
year = "1981",
doi = "10.1038/291167a0",
language = "English (US)",
volume = "291",
pages = "167--168",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "5811",

}

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 -