Heat stability of a tetrameric enzyme, D-glyceraldehyde-3-phosphate dehydrogenase.

@article{Walker1980HeatSO,
  title={Heat stability of a tetrameric enzyme, D-glyceraldehyde-3-phosphate dehydrogenase.},
  author={John E Walker and Alan J. Wonacott and J. Ieuan Harris},
  journal={European journal of biochemistry},
  year={1980},
  volume={108 2},
  pages={581-6}
}
The tetrameric enzyme D-glyceraldehyde-3-phosphate dehydrogenase from the moderate thermophile Bacillus stearothermophilus is more stable to thermal denaturation than its counterpart from lobster muscle [Harris et al. (1980) Eur. J. Biochem. 108, 535-547]. Extra buried ionic bonds between subunits of the thermophilic enzyme make an important contribution to thermal stabilisation. Further stabilisatio of the tetrameric enzyme is derived from additional hydrophobic interactions between the S… CONTINUE READING