Sandbox Reserved 771
This Sandbox is Reserved from Sep 25, 2013, through Mar 31, 2014 for use in the course "BCH455/555 Proteins and Molecular Mechanisms" taught by Michael B. Goshe at the North Carolina State University. This reservation includes Sandbox Reserved 299, Sandbox Reserved 300 and Sandbox Reserved 760 through Sandbox Reserved 779. |
To get started:
More help: Help:Editing |
Glutathione synthetase (GSS) is an homo-dimeric, ATP-depending responsible for the condensation of γ-Glutamylcysteine and glycine to form Glutathione during the second step of the glutathione biosynthesis pathway. Glutathione considered to be one of the most abundant and important antioxidants present in mammalian cells. In addition to protecting cells from the oxidative damage caused by free radicals, it is believed to be involved in the detoxification of xenobiotics, as well as membrane transport. Below, the direct enzyme catalysis step is shown in addition to the entire glutathione biosynthesis pathway and GSS's role in such a cycle.
Reaction MechanismReaction Mechanism
Substrate and ATP Binding SitesSubstrate and ATP Binding Sites
Glycine TriadGlycine Triad
Alternative Splicing VariantsAlternative Splicing Variants
While the expression of glutathione synthetase (GSS) has been studied and fairly well characterized, the sequence and alternative splicing of the gss gene has been studied very little. Using real-time polymerase chain reaction (qPCR) to quantify mRNA levels of the gss transcript within human cells has revealed one common alternative splicing variant present within colon, kidney, lung, liver, placenta, blood, and uterus cells. It has not, however, been detected within heart, skeletal muscle, and spleen tissue cells. This ASV is produced from a 333 bp in-frame deletion, including the complete removal of exons 4 and 5.
Chronic Lung Infections Caused by Alterations to Glutathione SynthesisChronic Lung Infections Caused by Alterations to Glutathione Synthesis
ReferencesReferences
1. http://www.ncbi.nlm.nih.gov/protein/NP_000169.1
2. Dinescu A, Brown TR, Barelier S, Cundari TR, Anderson ME. 2010. The role of the glycine triad in human glutathione synthesis. Biochem Biophys Res Commun, 400(4):511-516. doi: 10.1016/j.bbrc.2010.08.081
3. Uchida M, Sugaya M, Janamary T, Hisatomi H. 2010. Alternative RNA splicing in expression of the glutathione synthetase gene in human cells. Mol Biol Rep, 37(4): 2105-2109. doi: 10.1007/s11033-009-9675-3
4. Breton CV, Salam MT, Vora H, Gauderman WJ, Gilliland FD. 2011. Genetic variation in the glutathione synthesis pathway, air pollution, and children's lung function growth. Amer Jour Respir Crit Care Med, 183(2): 243-248. doi: 10.1164/rccm.201006-0849OC