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Literature summary for 2.4.1.11 extracted from
- Structural basis for glucose-6-phosphate activation of glycogen synthase (2010), Proc. Natl. Acad. Sci. USA, 107, 17563-17568.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| glucose-6-phosphate | D-glucose 6-phosphate binding structure, Arg580 forms an interaction with the 6-phosphate of D-glucose 6-phosphate, overview. The eukaryotic enzyme is activated by protein phosphatases and D-glucose 6-phosphate binding. The enzyme's response to D-glucose 6-phosphate is controlled by Arg583 and Arg587, while four additional arginine residues present within the same regulatory helix regulate the response to phosphorylation | Saccharomyces cerevisiae |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-tagged wild-type and mutant Gsy2 proteins in Escherichia coli strain BL21(DE3) | Saccharomyces cerevisiae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant His-tagged enzyme, basal state and glucose-6-phosphate activated state Gsy2p, X-ray diffraction structure determination and analysis at 3.0 A and 2.4 A, respectively, modeling | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | generation of a wild-type 640 truncation mutant with increased activity compared to the wild-type, and of point mutation variants with nonphospho- and phospho-peptides ligated, which alters the mutant activities, overview | Saccharomyces cerevisiae |
| R580A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
| R580A/R581A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
| R580A/R581A/R583A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The triple mutant enzyme is resistant to inhibition by Pho85p/Pcl10p phosphorylation | Saccharomyces cerevisiae |
| R587A/R589A/R592A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
| R589A/R592A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the eukaryotic enzyme is inhibited by protein kinase mediated phosphorylation, four arginine residues of a regulatory helix regulate the response to phosphorylation. When Thr668 is phosphorylated, Arg580 and Arg581 play a role in stabilizing the inhibited conformation by directly interacting with the phosphate group at or near the N-terminus of the regulatory helix, possibly near one of the sulfate binding sites in our basal state structure | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-glucose + [(1->4)-alpha-D-glucosyl]n | Saccharomyces cerevisiae | - |
UDP + [(1->4)-alpha-D-glucosyl]n+1 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | the eukaryotic enzymes are inhibited by protein kinase mediated phosphorylation and activated by protein phosphatases and glucose-6-phosphate binding, regulation, overview | Saccharomyces cerevisiae |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant Gsy2 proteins from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-glucose + [(1->4)-alpha-D-glucosyl]n | - |
Saccharomyces cerevisiae | UDP + [(1->4)-alpha-D-glucosyl]n+1 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | - |
Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| glycogen synthase-2 | - |
Saccharomyces cerevisiae |
| Gys2p | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | glycogen synthase homologues in bacteria and archaea lack regulation, while the eukaryotic enzymes are inhibited by protein kinase mediated phosphorylation and activated by protein phosphatases and D-glucose 6-phosphate binding | Saccharomyces cerevisiae |
| additional information | in the basal activity state and D-glucose 6-phosphate activated state, the enzyme is assembled into an unusual tetramer by an insertion unique to the eukaryotic enzymes, and this subunit interface is rearranged by the binding of D-glucose 6-phosphate, which frees the active site cleft and facilitates catalysis. Structure function in enzyme regulation, overview | Saccharomyces cerevisiae |
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