Glycogen synthase: Difference between revisions
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Glycogen Synthase (GS) is an enzyme that catalyses the production of [[Glycogen| | Glycogen Synthase (GS) is an [[Enzyme|enzyme]] present in [[Liver|liver]] and muscle cells that catalyses the production of [[Glycogen|glycogen]]. It catalyses a [[Condensation Reaction|condensation reaction]] between [[UDP-glucose|UDP-glucose]] and glycogen (n-residues) to form [[Glycogen|glycogen]] (n+1 residues) and [[UDP|UDP]], elongating the glycogen polymer. <br> | ||
< | Regulation of the enzyme is achieved through multiple [[Phosphorylation|phosphorylations]] at different sites by multiples [[Kinase|kinases]], including [[Protein kinase B|Protein Kinase B]] (PKB) and [[Glycogen Synthase Kinase 3|Glycogen Synthase Kinase 3]] (GSK3). When insulin is absent from cells, GSK3 phosphorylates Glycogen Synthase, inactivating it, this maintains the level of glucose available to the cells. Upon [[Insulin|insulin]] stimulation, PKB is activated and phosphorylates GSK3, which is also a repressing phosphorylation. GSK3 can now no longer inhibit Glycogen Synthase, thereby increasing the concentration of glycogen and reducing the concentration of glucose within the cells <ref>Harvey Lodish, Arnold Berk, Chris A. Kaiser, Monty Krieger, Matthew P. Scott, Anthony Bretscher and Hidde Ploegh (2008) Molecular Cell Biology, sixth edition,United States of America: W. H. Freeman and Company</ref>. | ||
Insulin also activates a [[Phosphatase|phosphatase]] called [[Protein Phosphatase-1|Protein Phosphatase-1 (PP1)]], which [[Dephosphorylation|dephosphorylates]] GS. The pathway as to how this occurs is unclear. | |||
=== References === | |||
<references /> <br> | |||
Latest revision as of 21:14, 21 October 2012
Glycogen Synthase (GS) is an enzyme present in liver and muscle cells that catalyses the production of glycogen. It catalyses a condensation reaction between UDP-glucose and glycogen (n-residues) to form glycogen (n+1 residues) and UDP, elongating the glycogen polymer.
Regulation of the enzyme is achieved through multiple phosphorylations at different sites by multiples kinases, including Protein Kinase B (PKB) and Glycogen Synthase Kinase 3 (GSK3). When insulin is absent from cells, GSK3 phosphorylates Glycogen Synthase, inactivating it, this maintains the level of glucose available to the cells. Upon insulin stimulation, PKB is activated and phosphorylates GSK3, which is also a repressing phosphorylation. GSK3 can now no longer inhibit Glycogen Synthase, thereby increasing the concentration of glycogen and reducing the concentration of glucose within the cells [1].
Insulin also activates a phosphatase called Protein Phosphatase-1 (PP1), which dephosphorylates GS. The pathway as to how this occurs is unclear.
References
- ↑ Harvey Lodish, Arnold Berk, Chris A. Kaiser, Monty Krieger, Matthew P. Scott, Anthony Bretscher and Hidde Ploegh (2008) Molecular Cell Biology, sixth edition,United States of America: W. H. Freeman and Company