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Posttranslational Modification of Human Glyoxalase 1 Indicates Redox-Dependent Regulation
| Type: | Application |
Scientific Paper |
Clinical Proteomics |
| Number: | Technology |
10.1371/journal.pone.0010399 |
FTMS |
| Year | Products |
2010 |
BioApexII ESI-FTICR-MS |
| Author | |
Gerd Birkenmeier, Christin Stegemann, Ralf Hoffmann, Robert Gunther, Klaus Huse, Claudia Birkemeyer |
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| Reference | |
PLoS ONE |
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Abstract |
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It is shown for the first time that Glo1 activity directly can be regulated by an oxidative posttranslational modification that was found in the native enzyme, i.e., glutathionylation. Inhibition of Glo1 by chemical reaction with its co-factor and the role of its intramolecular disulfides are expected to be important factors within the context of redox-dependent regulation of glucose metabolism in cells.
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