Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima.

@article{Wrba1990ExtremelyTD,
  title={Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima.},
  author={A Wrba and Ana Paula Schweiger and V Schultes and Rainer Jaenicke and P{\'e}ter Z{\'a}vodszky},
  journal={Biochemistry},
  year={1990},
  volume={29 33},
  pages={7584-92}
}
D-Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Thermotoga maritima, a hyperthermophilic eubacterium, has been isolated in pure crystalline form. The enzyme is a homotetramer with a subunit molecular mass of 37 kDa. The sedimentation coefficient of the native enzyme is 7.3 X 10(-13)s, the isoelectric point is 4.6, and the specific absorption coefficient A1%, 1cm 280nm = 8.4. The enzyme shows extreme thermal stability: differential scanning calorimetry yields a transition temperature (Tm… CONTINUE READING