TM0688

Summary

Gene Symbol: TM0688
Description: glyceraldehyde-3-phosphate dehydrogenase
Species: Thermotoga maritima MSB8

Top Publications

  1. ncbi Complete amino-acid sequence of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
    V Schultes
    Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, Federal Republic of Germany
    Eur J Biochem 192:25-31. 1990
  2. ncbi The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 A resolution
    I Korndörfer
    Max Planck Institut fur Biochemie, Martinsried, FRG
    J Mol Biol 246:511-21. 1995
  3. ncbi Functional expression of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima in Escherichia coli. Authenticity and kinetic properties of the recombinant enzyme
    A Tomschy
    Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, Germany
    Eur J Biochem 214:43-50. 1993

Detail Information

Publications3

  1. ncbi Complete amino-acid sequence of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
    V Schultes
    Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, Federal Republic of Germany
    Eur J Biochem 192:25-31. 1990
    ..4. Thermal stability is caused by minute adjustments of the local three-dimensional structure. Previous 'strategies of thermal adaptation' in terms of preferred amino-acid exchanges are not in accordance with the present sequence data...
  2. ncbi The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 A resolution
    I Korndörfer
    Max Planck Institut fur Biochemie, Martinsried, FRG
    J Mol Biol 246:511-21. 1995
    ..A large number of extra salt-bridges may be an important factor contributing to the high thermostability of this protein...
  3. ncbi Functional expression of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima in Escherichia coli. Authenticity and kinetic properties of the recombinant enzyme
    A Tomschy
    Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, Germany
    Eur J Biochem 214:43-50. 1993
    ..The expressed protein restores the natural E. coli phenotype in a gap- strain, thus providing evidence that the hyperthermophilic protein can fold and associate to its native, functional state in its mesophilic host...