Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogen-binding site.

@article{Daz2011ProcessivityAS,
  title={Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogen-binding site.},
  author={Adelaida D{\'i}az and Carlos Mart{\'i}nez-Pons and Ignacio Fita and Juan C. Ferrer and Joan J. Guinovart},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 21},
  pages={18505-14}
}
Glycogen synthase, a central enzyme in glucose metabolism, catalyzes the successive addition of α-1,4-linked glucose residues to the non-reducing end of a growing glycogen molecule. A non-catalytic glycogen-binding site, identified by x-ray crystallography on the surface of the glycogen synthase from the archaeon Pyrococcus abyssi, has been found to be functionally conserved in the eukaryotic enzymes. The disruption of this binding site in both the archaeal and the human muscle glycogen… CONTINUE READING