Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Sci Signal. 2009 Nov 10;2(96):ra72. doi: 10.1126/scisignal.2000464.
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.
硫化氢(H2S)是由胱硫醚γ-裂解酶生成的信使分子,作为一种生理性血管舒张剂。H2S 信号的机制一直难以捉摸。我们现在表明,H2S 通过 S-巯基化在大量蛋白质中生理性修饰半胱氨酸。在生理条件下,约 10%至 25%的许多肝蛋白,包括肌动蛋白、微管蛋白和甘油醛-3-磷酸脱氢酶(GAPDH),都发生巯基化。巯基化增强 GAPDH 活性并增强肌动蛋白聚合。因此,巯基化似乎是蛋白质的一种生理性翻译后修饰。