Heat stability of maize endosperm ADP-glucose pyrophosphorylase is enhanced by insertion of a cysteine in the N terminus of the small subunit.

@article{Linebarger2005HeatSO,
  title={Heat stability of maize endosperm ADP-glucose pyrophosphorylase is enhanced by insertion of a cysteine in the N terminus of the small subunit.},
  author={Carla R Lyerly Linebarger and Susan K. Boehlein and Aileen K. Sewell and Janine R. Shaw and L. Curtis Hannah},
  journal={Plant physiology},
  year={2005},
  volume={139 4},
  pages={1625-34}
}
ADP-glucose pyrophosphorylase (AGPase) is a key regulatory enzyme in starch biosynthesis. However, plant AGPases differ in several parameters, including spatial and temporal expression, allosteric regulation, and heat stability. AGPases of cereal endosperms are heat labile, while those in other tissues, such as the potato (Solanum tuberosum) tuber, are heat stable. Sequence comparisons of heat-stable and heat-labile AGPases identified an N-terminal motif unique to heat-stable enzymes. Insertion… CONTINUE READING