Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus

@article{Biesecker1977SequenceAS,
  title={Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus},
  author={G E Biesecker and J. Ieuan Harris and J. C. Thierry and John E Walker and Alan J. Wonacott},
  journal={Nature},
  year={1977},
  volume={266},
  pages={328-333}
}
The glyceraldehyde 3-phosphate dehydogenase holoenzyme of Bacillus stearothermophilus possesses precise 222 symmetry: in this respect it differs from the reported structure of the lobster muscle enzyme. Pairs of active sites are linked through a flexible polypeptide loop which probably mediates the structural changes giving rise to cooperative effects… CONTINUE READING