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Literature summary extracted from

  • Linebarger, C.R.; Boehlein, S.K.; Sewell, A.K.; Shaw, J.; Hannah, L.C.
    Heat stability of maize endosperm ADP-glucose pyrophosphorylase is enhanced by insertion of a cysteine in the N-terminus of the small subunit (2005), Plant Physiol., 139, 1625-1634.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.27 3-phosphoglycerate
-
 Zea mays

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.27 S34E/Y36C significant increase in heat stability as compared to wild-type enzyme Zea mays
2.7.7.27 S34Q/Y36C significant increase in heat stability as compared to wild-type enzyme. The ratio of turnover-number to KM-value for ATP is 2.1fold higher than wild-type ratio, the ratio of turnover-number to KM-value for alpha-D-glucose 1-phosphate is 2.6fold higher than wild-type ratio Zea mays
2.7.7.27 Y36C significant increase in heat stability as compared to wild-type enzyme Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.27 phosphate
-
 Zea mays

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.27 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.27
-
 Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.27 endosperm
-
 Zea mays
-

Synonyms

EC Number Synonyms Comment Organism
2.7.7.27 ADP-glucose pyrophosphorylase
-
 Zea mays