Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase.

@article{Meng2009DomainspecificDO,
  title={Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase.},
  author={Meng Meng and Elisabeth Fitzek and Agnieszka Gajowniczek and Malgorzata Wilczynska and Leszek A. Kleczkowski},
  journal={Biochimica et biophysica acta},
  year={2009},
  volume={1794 12},
  pages={1734-42}
}
UDP-glucose (UDPG) pyrophosphorylase (UGPase) produces UDPG for sucrose and polysaccharide synthesis and glycosylation reactions. In this study, several barley UGPase mutants were produced, either single amino acid mutants or involving deletions of N- and C-terminal domains (Ncut and Ccut mutants, respectively) and of active site region ("NB loop"). The Del-NB mutant yielded no activity, whereas Ncut deletions and most of Ccut mutants, including short deletions at the so called "I-loop" region… CONTINUE READING
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