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QUESTION
GYS1 gene glycogen synthase 1
POSTER
1. References
= Pick a paper that deals with a defect from a particular enzyme
= What biochemical pathway does it follow
= should be a Core biochem study
= not too clinical
= only go back 10 years
= primary articles best
2. Poster
= Asking a key question and addressing in paper
= Biochemistry enzyme
= Structural info on enzyme in paper
= Modules included
= Clinical papers are secondary info
= discuss Importance of protein
= discuss During defect what goes wrong in pathway
3. Figures
= show representation of the enzyme
= Generate from chimera
= or used the one in attachment
4. Format
= AMA
Role of GYS1 gene glycogen synthase 1 in Glycogen Synthesis
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Nursing |
Pages |
5 |
Style |
APA |
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Answer
Enzyme
Glycogen synthase is regulated by allosteric activation of glucose-6-phosphate binding as well as the inactivation by phosphorylation on its C- and N- terminal regulatory tails. Glycogen synthase is incapable of initiating synthesis of a glycogen molecule de novo but it extends the pre-existing chains initiated by glycogenin. However, the molecular determinants by which glycogen synthase identify self-regulated glycogenin are unknown1. Conversion of glucose into glycogen is fundamental in glucose regulation1. Glycogen synthase 1 is a rate-limiting enzyme in glycogen synthesis.4 Glycose is stored in to form of glycogen and is a convenient form of glycose storage for use during periods of energy stress, senescence or deprivation4. Glycogen contains 55,000 glucose molecules linked together in as a chain, mostly in muscle cells and liver cells1.
Structure
Yeast and mammalian glycogen synthase belongs to the GT3 family of glycosyltransferases. On the other hand, plant and bacterial glycogen transferase belongs to the GT5 family. Both GT5 and GT3 families have GT-B architecture, which comprise of two tightly associated Rossmann fold chains3. Refer to Figure 1 and 2. The activity of glycogen synthase 1 is tightly suppressed by N-terminal (regulatory sites) phosphorylation Glycogen synthase 1 as well as phosphorylation at the C-terminal extensions1. The subunits include CeGS protomers (blue) [Refer to Figure 3] and the budding yeast ScGS (PDB ID code 3NAZ, gray). In Figure 3, the N-terminal extension of CeGS (green) and C-terminal extensions of CeGS (red) and ScGS (orange) are also highlighted. Phosphoregulatory sites 2 (S12), 2a (T19), 3a (S654), 3b (S658), and 3c (S662) and the allosteric regulatory site (Arg cluster) on the CeGS protomer are shown as ball and stick models with violet-colored carbon atoms1. Refer to Figure 3.
Enzyme Function
Glycogen-synthase is described as a rate-limiting-enzyme in glycogen synthesis3. Glycogen synthase catalyzes conversion of glucose molecules into glycogen. Glycogen. The enzyme synthesizes α-1,4-linked glucose polymers1. Glycogen synthase is allosterically activated by glucose 6-phophate and covalently regulated by phosphorylation3. Apart from glycogen synthesis, glycogen synthase promotes uptake of glucose into cells and can as well increase the rate of glycolysis. Glucose-6-phosphate is a known activator of glycogen synthase14.
Conclusion
Glycogen synthase 1 is catalyzes conversion of glucose into glycogen1. it also increases uptake of glucose into body cells and increases the rate of glycolysis4. Glycogen synthase 1 is a rate-limiting enzyme is glycogen synthases; thus, it is targeted in cancer therapies since high glucose levels drives proliferation of cancer cells4. Glycogen is the most convenient form of storage glucose surplus during periods of energy needs or crisis4. Apart from acting as energy storage form, conversion of glucose to glycogen is a fundamental process in glucose regulation in the body1. The enzyme structure can be described by Rossmann fold and associates with glycogen -6-phosphate and glycogenin to influence its function1,3.
References
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- Zeqiraj, E., Tang, Hunter, R. W., Garcia-Rocha, M., Judd, A., Deak, M., Wilamowitz-Moellendorff, A., Kurinov, I., Guinovart, J. J., Tyers, M., Sakamoto, K., & Sicheri, F. (2014). Structural basis for the recruitment of glycogen synthesis by glycogenin. Proc Natl Acad Sci U S A., 111(28), E2831-E2840. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4104858/
- Buschiazzo, A., Guerin, M. E., Ugalde, J. E., Shepard, W., & Alzari, P. M. (2017). 1RZV: Crystal structure of the glycogen synthase from Agrobacterium tumefaciens (non-complexed form). https://www.rcsb.org/structure/1RZV
- Mahalingan, K. K., Baskaran, S., DePaoli-Roach, A. A., Roach, P. J., & Hurley, T. D. (2017). Redox switch for the inhibited state of yeast glycogen synthase mimics regulation by phosphorylation. Biochemistry, 56(1), 179-188. https://pubs.acs.org/doi/abs/10.1021/acs.biochem.6b00884
- Bhanot, H., Reddy, M .M., Nonami, A., Weisberg, E. L., Bonal, D., Kirscmeier, P. T., Salgia, S., Podar, et al. (2015). Pathological glycogenesis through glycogen synthase 1 and suppression of excessive AMP kinase activity in myeloid leukemia cells. Luekemia, 29(7), 1555-1563. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4497855/
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