Glutathione S-transferases

biomedical applications

G J Beckett, J D Hayes

Research output: Contribution to journalReview article

259 Citations (Scopus)

Abstract

This chapter focuses on the biomedical applications of ubiquitous and modest size enzymes, glutathione S-transferases (GST), found in bacteria, yeast, nematodes, insects, fish, birds, and mammals. They constitute a complex supergene family that collectively metabolizes chemotherapeutic drugs, carcinogens, environmental pollutants, and a broad spectrum of other harmful foreign compounds (xenobiotics). The fact that GST is present at high levels in the liver ensures that their concentration in plasma provides an exceptionally sensitive index of hepatocellular damage. Whereas the function of GST is considered primarily to be one of detoxifying foreign compounds, these enzymes possess activities other than catalyzing the formation of glutathione–xenobiotic conjugates. For example, GST exhibit peroxidase activity toward organic hydroperoxides and serve to combat oxidative stress. The conjugation between reduced glutathione (GSH) and xenobiotics represents the few subsequent steps that lead to the formation of mercapturic acids: the removal of the γ-glutamyl moiety from the glutathione conjugate by γ-glutamyltransferase, the enzymatic removal of glycine from the cysteinyl glycine conjugate, and the N-acetylation of the cysteine conjugate by an acetyl-CoA-linked acetylase. The final N-acetylcysteine thioethers, or mercapturic acids, produced by the enzymes that catalyze this pathway are water soluble and are readily excreted from the body.

Original languageEnglish
Pages (from-to)281-380
Number of pages100
JournalAdvances in Clinical Chemistry
Volume30
DOIs
Publication statusPublished - 1993

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Glutathione Transferase
Acetylcysteine
Xenobiotics
cysteinylglycine
Glutathione
Enzymes
Acetylesterase
Acetylation
Environmental Pollutants
Carcinogens
Acetyl Coenzyme A
Mammals
Oxidative stress
Birds
Enzyme activity
Sulfides
Liver
Yeast
Glycine
Fish

Keywords

  • Animals
  • Glutathione Transferase/analysis
  • Humans
  • Hyperthyroidism/enzymology
  • Isoenzymes/analysis
  • Kidney/enzymology
  • Liver Diseases/enzymology
  • Neoplasms/enzymology

Cite this

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title = "Glutathione S-transferases: biomedical applications",
abstract = "This chapter focuses on the biomedical applications of ubiquitous and modest size enzymes, glutathione S-transferases (GST), found in bacteria, yeast, nematodes, insects, fish, birds, and mammals. They constitute a complex supergene family that collectively metabolizes chemotherapeutic drugs, carcinogens, environmental pollutants, and a broad spectrum of other harmful foreign compounds (xenobiotics). The fact that GST is present at high levels in the liver ensures that their concentration in plasma provides an exceptionally sensitive index of hepatocellular damage. Whereas the function of GST is considered primarily to be one of detoxifying foreign compounds, these enzymes possess activities other than catalyzing the formation of glutathione–xenobiotic conjugates. For example, GST exhibit peroxidase activity toward organic hydroperoxides and serve to combat oxidative stress. The conjugation between reduced glutathione (GSH) and xenobiotics represents the few subsequent steps that lead to the formation of mercapturic acids: the removal of the γ-glutamyl moiety from the glutathione conjugate by γ-glutamyltransferase, the enzymatic removal of glycine from the cysteinyl glycine conjugate, and the N-acetylation of the cysteine conjugate by an acetyl-CoA-linked acetylase. The final N-acetylcysteine thioethers, or mercapturic acids, produced by the enzymes that catalyze this pathway are water soluble and are readily excreted from the body.",
keywords = "Animals, Glutathione Transferase/analysis, Humans, Hyperthyroidism/enzymology, Isoenzymes/analysis, Kidney/enzymology, Liver Diseases/enzymology, Neoplasms/enzymology",
author = "Beckett, {G J} and Hayes, {J D}",
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language = "English",
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}

Glutathione S-transferases : biomedical applications. / Beckett, G J; Hayes, J D.

In: Advances in Clinical Chemistry, Vol. 30, 1993, p. 281-380.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Glutathione S-transferases

T2 - biomedical applications

AU - Beckett, G J

AU - Hayes, J D

PY - 1993

Y1 - 1993

N2 - This chapter focuses on the biomedical applications of ubiquitous and modest size enzymes, glutathione S-transferases (GST), found in bacteria, yeast, nematodes, insects, fish, birds, and mammals. They constitute a complex supergene family that collectively metabolizes chemotherapeutic drugs, carcinogens, environmental pollutants, and a broad spectrum of other harmful foreign compounds (xenobiotics). The fact that GST is present at high levels in the liver ensures that their concentration in plasma provides an exceptionally sensitive index of hepatocellular damage. Whereas the function of GST is considered primarily to be one of detoxifying foreign compounds, these enzymes possess activities other than catalyzing the formation of glutathione–xenobiotic conjugates. For example, GST exhibit peroxidase activity toward organic hydroperoxides and serve to combat oxidative stress. The conjugation between reduced glutathione (GSH) and xenobiotics represents the few subsequent steps that lead to the formation of mercapturic acids: the removal of the γ-glutamyl moiety from the glutathione conjugate by γ-glutamyltransferase, the enzymatic removal of glycine from the cysteinyl glycine conjugate, and the N-acetylation of the cysteine conjugate by an acetyl-CoA-linked acetylase. The final N-acetylcysteine thioethers, or mercapturic acids, produced by the enzymes that catalyze this pathway are water soluble and are readily excreted from the body.

AB - This chapter focuses on the biomedical applications of ubiquitous and modest size enzymes, glutathione S-transferases (GST), found in bacteria, yeast, nematodes, insects, fish, birds, and mammals. They constitute a complex supergene family that collectively metabolizes chemotherapeutic drugs, carcinogens, environmental pollutants, and a broad spectrum of other harmful foreign compounds (xenobiotics). The fact that GST is present at high levels in the liver ensures that their concentration in plasma provides an exceptionally sensitive index of hepatocellular damage. Whereas the function of GST is considered primarily to be one of detoxifying foreign compounds, these enzymes possess activities other than catalyzing the formation of glutathione–xenobiotic conjugates. For example, GST exhibit peroxidase activity toward organic hydroperoxides and serve to combat oxidative stress. The conjugation between reduced glutathione (GSH) and xenobiotics represents the few subsequent steps that lead to the formation of mercapturic acids: the removal of the γ-glutamyl moiety from the glutathione conjugate by γ-glutamyltransferase, the enzymatic removal of glycine from the cysteinyl glycine conjugate, and the N-acetylation of the cysteine conjugate by an acetyl-CoA-linked acetylase. The final N-acetylcysteine thioethers, or mercapturic acids, produced by the enzymes that catalyze this pathway are water soluble and are readily excreted from the body.

KW - Animals

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KW - Hyperthyroidism/enzymology

KW - Isoenzymes/analysis

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KW - Liver Diseases/enzymology

KW - Neoplasms/enzymology

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JO - Advances in Clinical Chemistry

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