Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
    Heat stability and allosteric properties of the maize endosperm ADP-glucose pyrophosphorylase are intimately intertwined (2008), Plant Physiol., 146, 289-299.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.27 3-phosphoglycerate
-
 Zea mays
2.7.7.27 fructose-6-phosphate
-
 Zea mays
2.7.7.27 Fruf-beta-(2->1)-6-O-P-Glcp
-
 Zea mays
2.7.7.27 glucose-6-phosphate
-
 Zea mays
2.7.7.27 glycerol phosphate
-
 Zea mays
2.7.7.27 additional information no activation by D-6-phosphogluconic acid, ribose 1,5-diphosphate, erythrose 4-phosphate, or methyl phosphate at 20 mM Zea mays
2.7.7.27 phosphoenolpyruvate
-
 Zea mays
2.7.7.27 ribose-5-phosphate
-
 Zea mays

General Stability

EC Number General Stability Organism
2.7.7.27 phosphate, in the absence of 3-PGA, stabilizes endosperm AGPase Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.27 phosphate phosphate binds tightly to the endosperm AGPase, but does not inhibit catalytic activity, it acts by displacing bound activators and returning the enzyme to its activity in their absence. Phosphate, in the absence of 3-PGA, also stabilizes maize endosperm AGPase Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.27 additional information
-
 additional information ordered kinetic mechanism, regulation of AGPase by effectors, detailed overview Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.27 ATP + alpha-D-glucose 1-phosphate Zea mays AGPase, a key regulatory enzyme in starch biosynthesis, is highly regulated, effects of substrates, detailed overview ADP-D-glucose + diphosphate
-
 r

Organism

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

Source Tissue

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

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
-
 Zea mays ADP-D-glucose + diphosphate
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate AGPase, a key regulatory enzyme in starch biosynthesis, is highly regulated, effects of substrates, detailed overview Zea mays ADP-D-glucose + diphosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.7.27 More the enzyme exists in two forms that have significantly different stabilities and do not interconvert rapidly Zea mays

Synonyms

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.7.27 additional information
-
 ATP and ADP-Glc, but not Glc-1-P and diphosphate, protect AGPase from thermal inactivation, 3-PGA acts synergistically, overview Zea mays