Theoretical and Applied Genetics

, Volume 128, Issue 10, pp 1893–1916 | Cite as

AGPase: its role in crop productivity with emphasis on heat tolerance in cereals

  • Gautam Saripalli
  • Pushpendra Kumar Gupta


Key message

AGPase, a key enzyme of starch biosynthetic pathway, has a significant role in crop productivity. Thermotolerant variants of AGPase in cereals may be used for developing cultivars, which may enhance productivity under heat stress.


Improvement of crop productivity has always been the major goal of plant breeders to meet the global demand for food. However, crop productivity itself is influenced in a large measure by a number of abiotic stresses including heat, which causes major losses in crop productivity. In cereals, crop productivity in terms of grain yield mainly depends upon the seed starch content so that starch biosynthesis and the enzymes involved in this process have been a major area of investigation for plant physiologists and plant breeders alike. Considerable work has been done on AGPase and its role in crop productivity, particularly under heat stress, because this enzyme is one of the major enzymes, which catalyses the rate-limiting first committed key enzymatic step of starch biosynthesis. Keeping the above in view, this review focuses on the basic features of AGPase including its structure, regulatory mechanisms involving allosteric regulators, its sub-cellular localization and its genetics. Major emphasis, however, has been laid on the genetics of AGPases and its manipulation for developing high yielding cultivars that will have comparable productivity under heat stress. Some important thermotolerant variants of AGPase, which mainly involve specific amino acid substitutions, have been highlighted, and the prospects of using these thermotolerant variants of AGPase in developing cultivars for heat prone areas have been discussed. The review also includes a brief account on transgenics for AGPase, which have been developed for basic studies and crop improvement.


Heat Stress Large Subunit Starch Synthesis Disulphide Bridge Starch Biosynthesis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



National Academy of Science India (NASI) and Indian National Science Academy (INSA), New Delhi, India, awarded Senior Scientist Fellowships to PKG, during the tenures of which this review was written. SG is thankful to Department of Biotechnology, Government of India, New Delhi, for the award of a Senior Research Fellowship. Authors are also thankful to Professor L.C.Hannah, University of Florida, for his comments and suggestions which helped in improving the manuscript.

Conflict of interest

No conflict of interest declared.


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© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Molecular Biology Laboratory, Department of Genetics and Plant BreedingCh.Charan Singh UniversityMeerutIndia

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