Substitution of tyrosine residues at the aromatic cluster around the betaA-betaB loop of rubisco small subunit affects the structural stability of the enzyme and the in vivo degradation under stress conditions.

@article{Esquvel2006SubstitutionOT,
  title={Substitution of tyrosine residues at the aromatic cluster around the betaA-betaB loop of rubisco small subunit affects the structural stability of the enzyme and the in vivo degradation under stress conditions.},
  author={M G Esqu{\'i}vel and Teresa M. Pinto and Julia Mar{\'i}n-Navarro and Joaqu{\'i}n Moreno},
  journal={Biochemistry},
  year={2006},
  volume={45 18},
  pages={5745-53}
}
Ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) plays a central metabolic role in photosynthetic eukaryotes, and its catabolism is a crucial process for the nutrient economy of higher plants. The rubisco holoenzyme is assembled from eight chloroplast-encoded large subunits and eight nuclear-encoded small subunits. We have identified a cluster of conserved tyrosines at the interface between subunits (comprising Y67, Y68, and Y72 from the betaA-betaB loop of the small subunit and Y226… CONTINUE READING