Glutathione transferase zeta: Novel xenobiotic substrates and enzyme inactivation

M. W. Anders; Wayne B. Anderson; Huey Fen Tzeng; Philip G. Board

Glutathione transferase zeta: Novel xenobiotic substrates and enzyme inactivation

M. W. Anders^*, Wayne B. Anderson, Huey Fen Tzeng, Philip G. Board

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Glutathione transferase zeta (GSTZ1-1) catalyzes the biotransformation of a range of α-haloalkanoates and the isomerization of maleylacetoacetate to furmarylacetoacetate. The elimination half-life of DCA is increased in human subjects or rats given single or multiple doses of DCA, and the biotransformation of DCA to glyoxylate is decreased in liver cytosol isolated from rats given DCA. The DCA-induced decrease in its metabolism was shown to be due to the inactivation of rat, mouse, and human cytosolic GSTZ1-1 and with the inactivation of recombinant polymorphic variants of hGSTZ1-1. The inactivation of hGSTZ1-1 is accompanied by the covalent modification of the protein by [¹⁴C]DCA and [³⁵S]glutathione.

Original language	English
Pages (from-to)	211-216
Number of pages	6
Journal	Chemico-Biological Interactions
Volume	133
Issue number	1-3
Publication status	Published - 28 Feb 2001

Cite this

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title = "Glutathione transferase zeta: Novel xenobiotic substrates and enzyme inactivation",

abstract = "Glutathione transferase zeta (GSTZ1-1) catalyzes the biotransformation of a range of α-haloalkanoates and the isomerization of maleylacetoacetate to furmarylacetoacetate. The elimination half-life of DCA is increased in human subjects or rats given single or multiple doses of DCA, and the biotransformation of DCA to glyoxylate is decreased in liver cytosol isolated from rats given DCA. The DCA-induced decrease in its metabolism was shown to be due to the inactivation of rat, mouse, and human cytosolic GSTZ1-1 and with the inactivation of recombinant polymorphic variants of hGSTZ1-1. The inactivation of hGSTZ1-1 is accompanied by the covalent modification of the protein by [14C]DCA and [35S]glutathione.",

keywords = "Dichloroacetate, Enzyme inactivation, Glutathione transferase zeta, Maleylacetoacetate isomerase",

author = "Anders, {M. W.} and Anderson, {Wayne B.} and Tzeng, {Huey Fen} and Board, {Philip G.}",

year = "2001",

month = feb,

day = "28",

language = "English",

volume = "133",

pages = "211--216",

journal = "Chemico-Biological Interactions",

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TY - JOUR

T1 - Glutathione transferase zeta

T2 - Novel xenobiotic substrates and enzyme inactivation

AU - Anders, M. W.

AU - Anderson, Wayne B.

AU - Tzeng, Huey Fen

AU - Board, Philip G.

PY - 2001/2/28

Y1 - 2001/2/28

N2 - Glutathione transferase zeta (GSTZ1-1) catalyzes the biotransformation of a range of α-haloalkanoates and the isomerization of maleylacetoacetate to furmarylacetoacetate. The elimination half-life of DCA is increased in human subjects or rats given single or multiple doses of DCA, and the biotransformation of DCA to glyoxylate is decreased in liver cytosol isolated from rats given DCA. The DCA-induced decrease in its metabolism was shown to be due to the inactivation of rat, mouse, and human cytosolic GSTZ1-1 and with the inactivation of recombinant polymorphic variants of hGSTZ1-1. The inactivation of hGSTZ1-1 is accompanied by the covalent modification of the protein by [14C]DCA and [35S]glutathione.

AB - Glutathione transferase zeta (GSTZ1-1) catalyzes the biotransformation of a range of α-haloalkanoates and the isomerization of maleylacetoacetate to furmarylacetoacetate. The elimination half-life of DCA is increased in human subjects or rats given single or multiple doses of DCA, and the biotransformation of DCA to glyoxylate is decreased in liver cytosol isolated from rats given DCA. The DCA-induced decrease in its metabolism was shown to be due to the inactivation of rat, mouse, and human cytosolic GSTZ1-1 and with the inactivation of recombinant polymorphic variants of hGSTZ1-1. The inactivation of hGSTZ1-1 is accompanied by the covalent modification of the protein by [14C]DCA and [35S]glutathione.

KW - Dichloroacetate

KW - Enzyme inactivation

KW - Glutathione transferase zeta

KW - Maleylacetoacetate isomerase

UR - http://www.scopus.com/inward/record.url?scp=0003198476&partnerID=8YFLogxK

M3 - Article

SN - 0009-2797

VL - 133

SP - 211

EP - 216

JO - Chemico-Biological Interactions

JF - Chemico-Biological Interactions

IS - 1-3

ER -

Glutathione transferase zeta: Novel xenobiotic substrates and enzyme inactivation

Abstract

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