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J. Biochem, 1974, Vol. 76, No. 4 771-782
© 1974 Japanese Biochemical Society

research-article

Phosphoglycerate Kinase of Bacillus stearothermophilus

Koichi SUZUKI and Kazutomo IMAHORI

Department of Agricultural Chemistry, Faculty of Agriculture, University of Tokyo Bunkyo-ku, Tokyo

  1. Phosphoglycerate kinase [EC 2.7.2.3 [EC] [EC] ] was isolated in a homogeneous form from thermophilic bacteria, Bacillus stearothermophilus, and some properties were examined.
  2. The enzyme was composed of a single polypeptide chain of molecular weight 42,000. The thermophilic enzyme had many properties in common with enzymes from mesophilic sources, e.g., pH optimum, kinetic properties, physical structure, amino acid composition, etc., though it was more stable against heat and urea denaturation.
  3. Analyses of the secondary structure of the enzyme showed that it was composed of 45% ß-structure, 20% {alpha}-helix, and 35% random coil.
  4. Titration of SH groups indicated that there was a single SH group in the molecule. The SH group reacted with various SH reagents only in the presence of denaturing reagent and did not seem to participate in the catalytic function.
  5. A classification of PGK into two classes is proposed based on the number and reactivity of SH groups.


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