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Literature summary extracted from

  • Kleczkowski, L.A.; Villand, P.; Lönneborg, A.; Olsen O.A.; Lüthi, E.
    Plant ADP-glucose pyrophosphoylase - recent advances and biotechnological perspectives (1991), Z. Naturforsch. C, 46c, 605-612.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.27 3-phosphoglycerate activation Escherichia coli
2.7.7.27 3-phosphoglycerate activation Hordeum vulgare
2.7.7.27 3-phosphoglycerate activation Spinacia oleracea
2.7.7.27 3-phosphoglycerate activation Zea mays
2.7.7.27 3-phosphoglycerate activation Solanum tuberosum
2.7.7.27 3-phosphoglycerate activation Oryza sativa
2.7.7.27 3-phosphoglycerate strong Hordeum vulgare
2.7.7.27 3-phosphoglycerate strong Spinacia oleracea
2.7.7.27 3-phosphoglycerate strong Zea mays
2.7.7.27 3-phosphoglycerate strong Solanum tuberosum
2.7.7.27 3-phosphoglycerate strong Oryza sativa
2.7.7.27 ADP activation, less effective than 3-phosphoglycerate Escherichia coli
2.7.7.27 ADP activation, less effective than 3-phosphoglycerate Hordeum vulgare
2.7.7.27 ADP activation, less effective than 3-phosphoglycerate Spinacia oleracea
2.7.7.27 ADP activation, less effective than 3-phosphoglycerate Zea mays
2.7.7.27 ADP activation, less effective than 3-phosphoglycerate Solanum tuberosum
2.7.7.27 ADP activation, less effective than 3-phosphoglycerate Oryza sativa
2.7.7.27 AMP activation, less effective than 3-phosphoglycerate Escherichia coli
2.7.7.27 AMP activation, less effective than 3-phosphoglycerate Hordeum vulgare
2.7.7.27 AMP activation, less effective than 3-phosphoglycerate Spinacia oleracea
2.7.7.27 AMP activation, less effective than 3-phosphoglycerate Zea mays
2.7.7.27 AMP activation, less effective than 3-phosphoglycerate Solanum tuberosum
2.7.7.27 AMP activation, less effective than 3-phosphoglycerate Oryza sativa
2.7.7.27 D-fructose 1,6-bisphosphate
-
 Escherichia coli
2.7.7.27 D-fructose 1,6-bisphosphate
-
 Hordeum vulgare
2.7.7.27 D-fructose 1,6-bisphosphate
-
 Spinacia oleracea
2.7.7.27 D-fructose 1,6-bisphosphate
-
 Zea mays
2.7.7.27 D-fructose 1,6-bisphosphate
-
 Solanum tuberosum
2.7.7.27 D-fructose 1,6-bisphosphate
-
 Oryza sativa
2.7.7.27 D-fructose 6-phosphate activation Escherichia coli
2.7.7.27 D-fructose 6-phosphate activation Hordeum vulgare
2.7.7.27 D-fructose 6-phosphate activation Spinacia oleracea
2.7.7.27 D-fructose 6-phosphate activation Zea mays
2.7.7.27 D-fructose 6-phosphate activation Solanum tuberosum
2.7.7.27 D-fructose 6-phosphate activation Oryza sativa
2.7.7.27 D-glucose 6-phosphate activation Escherichia coli
2.7.7.27 D-glucose 6-phosphate activation Hordeum vulgare
2.7.7.27 D-glucose 6-phosphate activation Spinacia oleracea
2.7.7.27 D-glucose 6-phosphate activation Zea mays
2.7.7.27 D-glucose 6-phosphate activation Solanum tuberosum
2.7.7.27 D-glucose 6-phosphate activation Oryza sativa
2.7.7.27 pyridoxal 5'-phosphate activation Escherichia coli
2.7.7.27 pyridoxal 5'-phosphate activation Hordeum vulgare
2.7.7.27 pyridoxal 5'-phosphate activation Spinacia oleracea
2.7.7.27 pyridoxal 5'-phosphate activation Zea mays
2.7.7.27 pyridoxal 5'-phosphate activation Solanum tuberosum
2.7.7.27 pyridoxal 5'-phosphate activation Oryza sativa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.27 survey of plant species and tissues from which cDNA sequences encoding the small and large subunit of ADPG pyrophosphorylase are available Hordeum vulgare
2.7.7.27 survey of plant species and tissues from which cDNA sequences encoding the small and large subunit of ADPG pyrophosphorylase are available Spinacia oleracea
2.7.7.27 survey of plant species and tissues from which cDNA sequences encoding the small and large subunit of ADPG pyrophosphorylase are available Zea mays
2.7.7.27 survey of plant species and tissues from which cDNA sequences encoding the small and large subunit of ADPG pyrophosphorylase are available Solanum tuberosum
2.7.7.27 survey of plant species and tissues from which cDNA sequences encoding the small and large subunit of ADPG pyrophosphorylase are available Oryza sativa

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.27 phosphate
-
 Escherichia coli
2.7.7.27 phosphate
-
 Hordeum vulgare
2.7.7.27 phosphate
-
 Oryza sativa
2.7.7.27 phosphate
-
 Solanum tuberosum
2.7.7.27 phosphate
-
 Spinacia oleracea
2.7.7.27 phosphate
-
 Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.27 amyloplast
-
 Hordeum vulgare 9501
-
2.7.7.27 amyloplast
-
 Spinacia oleracea 9501
-
2.7.7.27 amyloplast
-
 Zea mays 9501
-
2.7.7.27 amyloplast
-
 Oryza sativa 9501
-
2.7.7.27 amyloplast potato leaf Solanum tuberosum 9501
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.27 Mg2+ requirement Escherichia coli
2.7.7.27 Mg2+ requirement Hordeum vulgare
2.7.7.27 Mg2+ requirement Spinacia oleracea
2.7.7.27 Mg2+ requirement Zea mays
2.7.7.27 Mg2+ requirement Solanum tuberosum
2.7.7.27 Mg2+ requirement Oryza sativa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.27 210000 240000
-
 Hordeum vulgare
2.7.7.27 210000 240000
-
 Spinacia oleracea
2.7.7.27 210000 240000
-
 Zea mays
2.7.7.27 210000 240000
-
 Solanum tuberosum
2.7.7.27 210000 240000
-
 Oryza sativa

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.27 Escherichia coli
-
-
-
2.7.7.27 Hordeum vulgare
-
-
-
2.7.7.27 Oryza sativa
-
-
-
2.7.7.27 Solanum tuberosum
-
-
-
2.7.7.27 Spinacia oleracea
-
-
-
2.7.7.27 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.27
-
 Spinacia oleracea

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.27 endosperm
-
 Escherichia coli
-
2.7.7.27 endosperm
-
 Hordeum vulgare
-
2.7.7.27 endosperm
-
 Spinacia oleracea
-
2.7.7.27 endosperm
-
 Solanum tuberosum
-
2.7.7.27 endosperm
-
 Oryza sativa
-
2.7.7.27 endosperm maize Zea mays
-
2.7.7.27 leaf
-
 Escherichia coli
-
2.7.7.27 leaf
-
 Hordeum vulgare
-
2.7.7.27 leaf
-
 Spinacia oleracea
-
2.7.7.27 leaf
-
 Zea mays
-
2.7.7.27 leaf
-
 Solanum tuberosum
-
2.7.7.27 leaf
-
 Oryza sativa
-
2.7.7.27 tuber
-
 Solanum tuberosum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
 Escherichia coli diphosphate + ADP-glucose
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
 Hordeum vulgare diphosphate + ADP-glucose
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
 Spinacia oleracea diphosphate + ADP-glucose
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
 Zea mays diphosphate + ADP-glucose
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
 Solanum tuberosum diphosphate + ADP-glucose
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
 Oryza sativa diphosphate + ADP-glucose
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.7.27 heterotetramer plant enzymes, composed of two large, 51000-60000 Da, and two small subunits, 50000-55000 Da Hordeum vulgare
2.7.7.27 heterotetramer plant enzymes, composed of two large, 51000-60000 Da, and two small subunits, 50000-55000 Da Spinacia oleracea
2.7.7.27 heterotetramer plant enzymes, composed of two large, 51000-60000 Da, and two small subunits, 50000-55000 Da Zea mays
2.7.7.27 heterotetramer plant enzymes, composed of two large, 51000-60000 Da, and two small subunits, 50000-55000 Da Solanum tuberosum
2.7.7.27 heterotetramer plant enzymes, composed of two large, 51000-60000 Da, and two small subunits, 50000-55000 Da Oryza sativa
2.7.7.27 homotetramer
-
 Escherichia coli
2.7.7.27 homotetramer bacterial enzyme is composed of four equally-sized subunits Hordeum vulgare
2.7.7.27 homotetramer bacterial enzyme is composed of four equally-sized subunits Spinacia oleracea
2.7.7.27 homotetramer bacterial enzyme is composed of four equally-sized subunits Zea mays
2.7.7.27 homotetramer bacterial enzyme is composed of four equally-sized subunits Solanum tuberosum
2.7.7.27 homotetramer bacterial enzyme is composed of four equally-sized subunits Oryza sativa