Abstract
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.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Animals
-
Binding Sites
-
Drosophila melanogaster / enzymology*
-
Drosophila melanogaster / genetics
-
Drosophila melanogaster / metabolism
-
Genes, Insect
-
Glutathione / metabolism*
-
Glutathione Disulfide / metabolism
-
Glutathione Reductase / metabolism*
-
Humans
-
Kinetics
-
Molecular Sequence Data
-
Mutation
-
NADP / metabolism
-
Oxidation-Reduction
-
Sequence Alignment
-
Species Specificity
-
Substrate Specificity
-
Thioredoxin-Disulfide Reductase / antagonists & inhibitors
-
Thioredoxin-Disulfide Reductase / chemistry
-
Thioredoxin-Disulfide Reductase / genetics*
-
Thioredoxin-Disulfide Reductase / metabolism*
Substances
-
NADP
-
Glutathione Reductase
-
Thioredoxin-Disulfide Reductase
-
Glutathione
-
Glutathione Disulfide