scholarly journals Biosynthesis of Starch: ADPglucose Pyrophosphorylase, the Regulatory Enzyme of Starch Synthesis: Structure-Function Relationships.

1993 ◽  
Vol 40 (2) ◽  
pp. 117-131
Author(s):  
Jack PREISS
Keyword(s):  
Structure Function ◽  
Starch Synthesis ◽  
Adpglucose Pyrophosphorylase

scholarly journals Characterization of transgenic potato (Solanum tuberosum) tubers with increased ADPglucose pyrophosphorylase*

1996 ◽  
Vol 320 (2) ◽  
pp. 487-492 ◽  
Author(s):  
Lee J. SWEETLOVE ◽  
Michael M. BURRELL ◽  
Tom ap REES
Keyword(s):  
Solanum Tuberosum ◽  
Starch Synthesis ◽  
Transgenic Potato ◽  
Soluble Starch ◽  
Inorganic Pyrophosphatase ◽  
Cell Fractionation ◽  
Intracellular Location ◽  
Adpglucose Pyrophosphorylase ◽  
Patatin Promoter ◽  
Udpglucose Pyrophosphorylase

The aim of the work described in this paper was to characterize the tubers of potato (Solanum tuberosum var. Prairie) plants that had been transformed with the Escherichiacoli ADPglucose pyrophosphorylase (EC 2.7.7.27) gene, glgC-16, under the control of a patatin promoter. Over 30 lines of transformed plants with increased ADPglucose pyrophosphorylase activity were obtained. The tubers of six of these lines were compared with those of control plants expressing the gene for β-glucuronidase. The average increase in pyrophosphorylase activity was 200%, and the highest was 400%. Western immunoblotting of tuber extracts showed that the amounts of glgC-16 protein were linearly related to the extractable activity of the ADPglucose pyrophosphorylase. Cell fractionation studies showed that the increased activity of the pyrophosphorylase in the glgC-16 tubers had a similar intracellular location, the amyloplast fraction, to that found in the control tubers. No pleiotropic changes in the maximum catalytic activities of the following enzymes could be detected in the glgC-16 tubers: sucrose synthase, fructokinase, UDPglucose pyrophosphorylase, phosphofructokinase, soluble starch synthase, starch branching enzyme, phosphoglucomutase and alkaline inorganic pyrophosphatase. The glgC-16 tubers are held to be suitable for the study of the role of ADPglucose pyrophosphorylase in the control of starch synthesis.

Salt Tolerance and Regulation of Enzymes of Starch Synthesis in Cassava (Manihot esculenta Crantz)

1982 ◽  
Vol 9 (5) ◽  
pp. 509 ◽  
Author(s):  
JS Hawker ◽  
GM Smith
Keyword(s):  
Manihot Esculenta ◽  
Starch Synthesis ◽  
Starch Synthase ◽  
Manihot Esculenta Crantz ◽  
Adpglucose Pyrophosphorylase ◽  
Storage Organs ◽  
Porous Growth ◽  
Phosphoglyceric Acid ◽  
And Storage ◽  
Nutrient Solutions

The growth rate of cassava plants (Manihot esculenta cv. MAUS7) decreased with increasing concentrations of NaCl from 0 to 75 mM in nutrient solutions supplied regularly in a porous growth medium in a glasshouse. Tuber weight was reduced to one-half between 30 and 50 mM NaCl and there was some burning of apical leaves at 50 and 75 mM NaCl. By comparison with other plants, this cultivar of cassava can be considered to have medium sensitivity to salinity. Na+ and Cl- concentrations increased in all tissues with increasing concentrations of supplied NaCl, except that Na+ remained low in laminae until the 75 mM treatment. K+ levels decreased in tubers. Starch concentrations remained the same in tubers, and K+ stimulated starch bound ADPglucose starch synthase by 1 .5-fold. Leaves and tubers contained activities of ADPglucose pyrophosphorylase and ADPglucose-starch synthase similar to those found in leaves and storage organs of other starch synthesizing plants. ADPglucose pyrophosphorylase from leaves was stimulated 20-fold by 3-phosphoglyceric acid (3PGA) while the enzyme from tubers was almost completely dependent on 3PGA at pH 8.5. The A0.5 values for 3PGA (the concentration required for one-half maximal activation) for the leaf and tuber enzymes at pH 8.5 were 1.31 mM and 7.41 mM respectively. At pH 7.5 the leaf enzyme was stimulated 26-fold and the tuber enzyme was again almost completely dependent on 3PGA. The A0.5 values at pH 7.5 were 1.17 mM and 3.8 mM, respectively. The I0.5 values for PI (concentrations required to cause 50% inhibition) in the presence of 3PGA were 2 mM, 0.25 mM and 0.04 mM for leaf enzyme at pH 8.5 and tuber enzyme at pH 8.5 and 7.7 respectively. The results support the view that it is not possible to generalize about the magnitude of the control of ADPglucose synthesis in leaves as opposed to non-chlorophyllous tissues.

Starch synthesis in potato tubers transformed with the wheat genes for ADPglucose pyrophosphorylase

2002 ◽  
Vol 29 (8) ◽  
pp. 975 ◽  
Author(s):  
Kathryn A. Vardy ◽  
Michael J. Emes ◽  
Michael M. Burrell
Keyword(s):  
Solanum Tuberosum L ◽  
Starch Content ◽  
Starch Synthesis ◽  
Small Subunit ◽  
Starch Biosynthesis ◽  
Potato Tubers ◽  
Potato Plants ◽  
Adpglucose Pyrophosphorylase ◽  
Plastid Targeting

The aim of this work was to study the role of ADPglucose pyrophosphorylase (AGPase) in starch biosynthesis of non-photosynthetic organs. Agrobacterium tumefaciens was used to transform potato plants (Solanum tuberosum L. cv. Desire�) with the wheat AGPase genes (AGP-S and AGP-L, coding for the small and large subunits, respectively). Neither of these genes contains a recognisable plastid targeting sequence. Southern analysis and analysis of starch content identified four lines that contained both wheat sequences. Immunoblotting indicated that, in the tubers, three lines expressed the wheat small subunit (AGP-S), but AGP-L cross-reacting protein was not apparent. The fourth transgenic line had reduced AGPase activity. AGPase activity in the AGP-transgenic tubers ranged from 15 to 165% of that found in β-glucuronidase (GUS) control lines.

High Temperature Affects the Activity of Enzymes in the Committed Pathway of Starch Synthesis in Developing Wheat Endosperm

1993 ◽  
Vol 20 (2) ◽  
pp. 197 ◽  
Author(s):  
JS Hawker ◽  
CF Jenner
Keyword(s):  
High Temperature ◽  
Sucrose Synthase ◽  
Starch Synthesis ◽  
Dry Weight ◽  
Grain Filling ◽  
Soluble Starch ◽  
Starch Synthase ◽  
Adpglucose Pyrophosphorylase ◽  
Udpglucose Pyrophosphorylase ◽  
Lower Temperature

Ears of wheat were exposed for up to 10 days during the grain-filling stage to high temperature (35�C) and activities of five enzymes in the sucrose to starch pathway were compared to those in ears maintained at lower temperature (21�C day/16�C night). Two cultivars of wheat known to differ in their post-anthesis tolerance of high temperature were compared. On a per grain basis, the activity of sucrose synthase and of ADPglucose pyrophosphorylase in ears maintained at 21/16�C throughout did not change greatly between days 16 and 32 after anthesis, whereas UDPglucose pyrophosphorylase and soluble starch synthase activities declined with advancing development. Soluble starch synthase activity in grains of heated ears was decreased within 1 day to about one- half of the value in unheated grains, and 3 days' additional heating did not reduce the activity much further. Insoluble starch synthase activity was not significantly reduced by heating. Compared to soluble starch synthase, ADPglucose pyrophosphorylase activity was more slowly affected and decreased to a lesser extent by heat. Sucrose synthase and UDPglucose pyrophosphorylase activities were either not affected or only slightly reduced; part of this reduction could be due to advanced development at the higher temperature. In recovery experiments ears were heated for brief periods and then returned to 21/16�C for a few days. ADPglucose pyrophosphorylase and soluble starch synthase activities recovered in the cooler conditions but the other two enzymes generally only maintained or lost further activity. From a comparison of the activities of these enzymes with the rate of starch deposition, and by taking into account the effects of heating, it is proposed that the influence of heating on final grain dry weight is attributable to the observed reductions of soluble starch synthase activity.

scholarly journals Starch metabolism in tubers of transgenic potato (Solanum tuberosum) with increased ADPglucose pyrophosphorylase*

1996 ◽  
Vol 320 (2) ◽  
pp. 493-498 ◽  
Author(s):  
Lee J. SWEETLOVE ◽  
Michael M. BURRELL ◽  
Tom ap REES
Keyword(s):  
Solanum Tuberosum ◽  
Starch Content ◽  
Starch Synthesis ◽  
Fold Increase ◽  
Transgenic Potato ◽  
Detectable Effect ◽  
Adpglucose Pyrophosphorylase ◽  
Response Coefficient ◽  
Transgenic Lines

The aim of this work was to use tubers from transgenic lines of potato (Solanum tuberosum) containing increased amounts of ADPglucose pyrophosphorylase to study the role of this enzyme in the control of starch synthesis. A 4–5-fold increase in activity of the enzyme, achieved by transformation with the Escherichia coli ADPglucose pyrophosphorylase gene glgC-16, had no detectable effect on the starch content of developing or mature tubers. No significant effects were found on the contents of ADPglucose, UDPglucose, glucose 1-phosphate, glucose 6-phosphate, PPi, ATP and ADP. Flux from [U-14C]sucrose, supplied to tubers still attached to the plant, to starch increased roughly in proportion to the increase in ADPglucose pyrophosphorylase activity. These measurements of flux gave a response coefficient close to 1 for the activity of the pyrophosphorylase in respect of starch synthesis. Pulse–chase experiments with [U-14C]sucrose showed that the increased flux into starch in the transformed tubers was accompanied by an increased rate of starch turnover. Further experiments suggested that the increased turnover was associated with an increase in the capacity of the tubers to degrade starch.

scholarly journals Structure‐Function Studies of the ADPGlucose Pyrophosphorylase from Thermodesulfovibrio yellowstonii

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Michael Susoeff ◽  
Eric Yik ◽  
Sandeep Kaur ◽  
Guatam Dua ◽  
Matthew Badal ◽  
...  
Keyword(s):  
Structure Function ◽  
Adpglucose Pyrophosphorylase
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