Purification and some properties of hydroxypyruvate isomerase of Bacillus fastidiosus

Biochim Biophys Acta. 1980 Jun 13;613(2):556-62. doi: 10.1016/0005-2744(80)90111-4.


Hydroxypyruvate isomerase of Bacillus fastidiosus is a novel enzyme (Braun, W. and Kaltwasser, H. (1979) Arch. Microbiol. 121, 129-134) which catalyzes the reversible conversion of tartronate semialdehyde into hydroxypyruvate. The enzyme was purified to homogeneity. The native molecule had a molecular weight of 265 000-280 000 and was composed of six subunits with a molecular weight of 45 000. The enzyme showed optimal activity at pH 6.6-7.4 and 57 degrees C. Hydroxypyruvate isomerase is stable on heating for 10 min at 67 degrees C. The enzyme appeared to be specific for tartronate semialdehyde and hydroxypyyruvate and no cofactors were involved in the reaction. The equilibrium constant K = [tartronate semialdehyde] divided by [hydroxypyruvate] was found to be 2.5 at pH 7.1, and 30 degrees C.

MeSH terms

  • Aldose-Ketose Isomerases*
  • Bacillus / enzymology*
  • Bacterial Proteins / isolation & purification*
  • Carbohydrate Epimerases / isolation & purification*
  • Carbohydrate Epimerases / metabolism
  • Catalysis
  • Escherichia coli Proteins*


  • Bacterial Proteins
  • Escherichia coli Proteins
  • Carbohydrate Epimerases
  • Aldose-Ketose Isomerases
  • hyi protein, E coli