Effects of mutations at residue 309 of the large subunit of ribulosebisphosphate carboxylase from Synechococcus PCC 6301.

@article{Morell1992EffectsOM,
  title={Effects of mutations at residue 309 of the large subunit of ribulosebisphosphate carboxylase from Synechococcus PCC 6301.},
  author={Matthew Morell and Heather Jean Kane and Graham S. Hudson and Timothy J. Andrews},
  journal={Archives of biochemistry and biophysics},
  year={1992},
  volume={299 2},
  pages={295-301}
}
Previous studies [G. S. Hudson et al. (1989) J. Biol. Chem. 265, 808-814] showed that the faster turnover rates and lower affinities for CO2 of ribulosebisphosphate carboxylase/oxygenases from C4 plants, compared to C3 and C3/C4 plants, were specified by the chloroplast-encoded large subunits. In pairs of closely related C3 and C4 species from three genera, these kinetic changes were accompanied by only three to six amino acid residue substitutions, depending on the genus. None of these… CONTINUE READING

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