Two ADP‐glucose pyrophosphorylase subunits, OsAGPL1 and OsAGPS1, modulate phosphorus homeostasis in rice

2020 ◽  
Vol 104 (5) ◽  
pp. 1269-1284
Author(s):  
Qi Meng ◽  
Wenqi Zhang ◽  
Xu Hu ◽  
Xinyu Shi ◽  
Lingling Chen ◽  
...  
Keyword(s):  
Adp Glucose Pyrophosphorylase

Increasing maize seed weight by enhancing the cytoplasmic ADP-glucose pyrophosphorylase activity in transgenic maize plants

2007 ◽  
Vol 88 (1) ◽  
pp. 83-92 ◽  
Author(s):  
Zhangying Wang ◽  
Xiaoping Chen ◽  
Jianhua Wang ◽  
Tingsong Liu ◽  
Yan Liu ◽  
...  
Keyword(s):  
Seed Weight ◽  
Transgenic Maize ◽  
Maize Seed ◽  
Maize Plants ◽  
Adp Glucose Pyrophosphorylase

Binding of 3-phosphoglycerate leads to both activation and stabilisation of ADP-glucose pyrophosphorylase from apple leaves

2005 ◽  
Vol 32 (9) ◽  
pp. 839
Author(s):  
Rui Zhou ◽  
Lailiang Cheng
Keyword(s):  
Heat Treatment ◽  
Thermal Stability ◽  
Enzyme Activity ◽  
Inorganic Phosphate ◽  
Thermal Inactivation ◽  
Specific Activity ◽  
Apple Leaves ◽  
Apparent Homogeneity ◽  
Adp Glucose Pyrophosphorylase ◽  
High Concentrations

Apple leaf ADP-glucose pyrophosphorylase was purified 1436-fold to apparent homogeneity with a specific activity of 58.9 units mg–1. The enzyme was activated by 3-phosphoglycerate (PGA) and inhibited by inorganic phosphate (Pi) in the ADPG synthesis direction. In the pyrophosphorolytic direction, however, high concentrations of PGA (> 2.5 mm) inhibited the enzyme activity. The enzyme was resistant to thermal inactivation with a T0.5 (temperature at which 50% of the enzyme activity is lost after 5 min incubation) of 52°C. Incubation with 2 mm PGA or 2 mm Pi increased T0.5 to 68°C. Incubation with 2 mm dithiothreitol (DTT) decreased T0.5 to 42°C, whereas inclusion of 2 mm PGA in the DTT incubation maintained T0.5 at 52°C. DTT-induced decrease in thermal stability was accompanied by monomerisation of the small subunits. Presence of PGA in the DTT incubation did not alter the monomerisation of the small subunits of the enzyme induced by DTT. These findings indicate that binding of PGA renders apple leaf AGPase with a conformation that is not only more efficient in catalysis but also more stable to heat treatment. The physiological significance of the protective effect of PGA on thermal inactivation of AGPase is discussed.

A colorimetric method for the assay of ADP-glucose pyrophosphorylase

2006 ◽  
Vol 352 (1) ◽  
pp. 145-147 ◽  
Author(s):  
Corina Fusari ◽  
Ana M. Demonte ◽  
Carlos M. Figueroa ◽  
Mabel Aleanzi ◽  
Alberto A. Iglesias
Keyword(s):  
Colorimetric Method ◽  
Adp Glucose Pyrophosphorylase
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