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Substitution of the Thioredoxin System for Glutathione Reductase in Drosophila melanogaster
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Substitution of the Thioredoxin System for Glutathione Reductase in Drosophila melanogaster
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Substitution of the Thioredoxin System for Glutathione Reductase in Drosophila melanogaster
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Journal Article
Substitution of the Thioredoxin System for Glutathione Reductase in Drosophila melanogaster
2001
Overview
The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals. These proteins maintain intracellular redox homeostasis to protect the organism from oxidative damage. Here we demonstrate the absence of glutathione reductase in Drosophila melanogaster, identify a new type of thioredoxin reductase, and provide evidence that a thioredoxin system supports GSSG reduction. Our data suggest that antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.
Publisher
American Society for the Advancement of Science,American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Analysis
/ Analytical, structural and metabolic biochemistry
/ Animals
/ Biological and medical sciences
/ DNA
/ Drosophila melanogaster - enzymology
/ Drosophila melanogaster - genetics
/ Drosophila melanogaster - metabolism
/ Enzymes
/ Enzymes and enzyme inhibitors
/ Fundamental and applied biological sciences. Psychology
/ Genes
/ genetics
/ Glutathione Disulfide - metabolism
/ Glutathione Reductase - metabolism
/ glutathione-disulfide reductase
/ Humans
/ Insects
/ Kinetics
/ Mutation
/ NADP
/ Proteins
/ Thioredoxin-Disulfide Reductase
/ Thioredoxin-Disulfide Reductase - antagonists & inhibitors
/ Thioredoxin-Disulfide Reductase - chemistry
