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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2011-1-12
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pubmed:abstractText |
The reversible oxidation of protein SH groups has been considered to be the basis of redox regulation by which changes in hydrogen peroxide (H2O2) concentrations may control protein function. Several proteins become S-glutathionylated following exposure to H2O2 in a variety of cellular systems. In yeast, when using a high initial H2O2 dose, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was identified as the major target of S-glutathionylation which leads to reversible inactivation of the enzyme. GAPDH inactivation by H2O2 functions to reroute carbohydrate flux to produce NADPH. Here we report the effect of low regulatory H2O2 doses on GAPDH activity and expression in Saccharomyces cerevisiae.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1471-2091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
49
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pubmed:dateRevised |
2011-7-20
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pubmed:meshHeading |
pubmed-meshheading:21189144-Animals,
pubmed-meshheading:21189144-Cell Cycle,
pubmed-meshheading:21189144-Dose-Response Relationship, Drug,
pubmed-meshheading:21189144-Enzyme Inhibitors,
pubmed-meshheading:21189144-Gene Expression Regulation, Fungal,
pubmed-meshheading:21189144-Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating),
pubmed-meshheading:21189144-Hydrogen Peroxide,
pubmed-meshheading:21189144-Isoenzymes,
pubmed-meshheading:21189144-Oxidation-Reduction,
pubmed-meshheading:21189144-Saccharomyces cerevisiae,
pubmed-meshheading:21189144-Up-Regulation
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pubmed:year |
2010
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pubmed:articleTitle |
Glyceraldehyde-3-phosphate dehydrogenase is largely unresponsive to low regulatory levels of hydrogen peroxide in Saccharomyces cerevisiae.
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pubmed:affiliation |
Centro de Química e Bioquímica, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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