| Literature DB >> 19903941 |
Asif K Mustafa1, Moataz M Gadalla, Nilkantha Sen, Seyun Kim, Weitong Mu, Sadia K Gazi, Roxanne K Barrow, Guangdong Yang, Rui Wang, Solomon H Snyder.
Abstract
Hydrogen sulfide (H2S), a messenger molecule generated by cystathionine gamma-lyase, acts as a physiologic vasorelaxant. Mechanisms whereby H2S signals have been elusive. We now show that H2S physiologically modifies cysteines in a large number of proteins by S-sulfhydration. About 10 to 25% of many liver proteins, including actin, tubulin, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), are sulfhydrated under physiological conditions. Sulfhydration augments GAPDH activity and enhances actin polymerization. Sulfhydration thus appears to be a physiologic posttranslational modification for proteins.Entities:
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Year: 2009 PMID: 19903941 PMCID: PMC2998899 DOI: 10.1126/scisignal.2000464
Source DB: PubMed Journal: Sci Signal ISSN: 1945-0877 Impact factor: 8.192