Abstract
The thioredoxin and glutathione systems play a central role in thiol-disulfide redox homeostasis in many organisms by providing electrons to essential enzymes, and defence against oxidative stress. These systems have recently been characterized in platyhelminth parasites, and the emerging biochemical scenario is the existence of linked processes with the enzyme thioredoxin glutathione reductase supplying reducing equivalents to both pathways. In contrast to their hosts, conventional thioredoxin reductase and glutathione reductase enzymes appear to be absent. Analysis of published data and expressed-sequence tag databases indicates the presence of linked thioredoxin-glutathione systems in the cytosolic and mitochondrial compartments of these parasites.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cytosol / enzymology
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Cytosol / metabolism
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Glutathione / genetics
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Glutathione / metabolism*
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Mitochondria / enzymology
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Mitochondria / metabolism
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Molecular Sequence Data
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Multienzyme Complexes / genetics
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Multienzyme Complexes / metabolism*
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NADH, NADPH Oxidoreductases / genetics
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NADH, NADPH Oxidoreductases / metabolism*
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Oxidation-Reduction
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Platyhelminths / enzymology
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Platyhelminths / genetics
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Platyhelminths / metabolism*
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Selenocysteine / metabolism
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Thioredoxins / genetics
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Thioredoxins / metabolism*
Substances
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Multienzyme Complexes
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Selenocysteine
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Thioredoxins
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NADH, NADPH Oxidoreductases
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thioredoxin glutathione reductase
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Glutathione