Activating Compound | Comment | Organism | Structure |
---|---|---|---|
fructose 6-phosphate | is an allosteric activator, binds to the interface between the N- and C-terminal domains, binding structure, modelling | Agrobacterium tumefaciens |
Cloned (Comment) | Organism |
---|---|
overexpression of selenomethionyl-labeled wild-type and mutant enzymes in glgC-Escherichia coli cells, strain TGC3 | Agrobacterium tumefaciens |
Crystallization (Comment) | Organism |
---|---|
purified recombinant selenomethionyl-labeled enzyme anomalous selenomethionyl derivative, sitting drop vapor diffusion method, lithium sulfate as a precipitant, samples containing 5 mg/ml protein are mixed with an equal volume of 1.5 M lithium sulfate and 100 mM HEPES, pH 7.5, as the mother liquor, 1 week, mother liquor containing 20% v/v glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 2.1 A resolution, modelling with ATP and alpha-D-glucose-1-phosphate bound to the active site, overview | Agrobacterium tumefaciens |
Protein Variants | Comment | Organism |
---|---|---|
H379K | site-directed mutagenesis, kinetics compared to the wild-type enzyme | Agrobacterium tumefaciens |
H379R | site-directed mutagenesis, kinetics compared to the wild-type enzyme | Agrobacterium tumefaciens |
additional information | site-directed mutagenesis of conserved glycines in this region, G20, G21, and G23, results in substantial loss of activity | Agrobacterium tumefaciens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
sulfate | is a competitive inhibitor for the allosteric activator fructose 6-phosphate, binds to the interface between the N- and C-terminal domains, binding structure, modelling | Agrobacterium tumefaciens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | wild-type and ADPGlc PPase H379R and ADPGlc PPase H379K mutant kinetics, overview | Agrobacterium tumefaciens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Agrobacterium tumefaciens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + alpha-D-glucose 1-phosphate | Agrobacterium tumefaciens | key step in glucan synthesis, the ADPGlc PPases are highly regulated by allosteric activators and inhibitors in accord with the carbon metabolism pathways of the organism | ADP-D-glucose + diphosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Agrobacterium tumefaciens | P39669 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant selenomethionyl-labeled wild-type and mutant enzymes from glgC-Escherichia coli cells, strain TGC3 | Agrobacterium tumefaciens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + alpha-D-glucose 1-phosphate | - |
Agrobacterium tumefaciens | ADP-D-glucose + diphosphate | - |
r | |
ATP + alpha-D-glucose 1-phosphate | key step in glucan synthesis, the ADPGlc PPases are highly regulated by allosteric activators and inhibitors in accord with the carbon metabolism pathways of the organism | Agrobacterium tumefaciens | ADP-D-glucose + diphosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | two domains: an N-terminal alpha/alpha sandwich and a C-terminal parallel beta-helix, ADPGlc PPase/fructose 6-phosphate structural model, overview | Agrobacterium tumefaciens |
Synonyms | Comment | Organism |
---|---|---|
ADP-glucose pyrophosphorylase | - |
Agrobacterium tumefaciens |
ADPGlc PPase | - |
Agrobacterium tumefaciens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Agrobacterium tumefaciens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Agrobacterium tumefaciens |