Purification and properties of an acid phosphatase of Micrococcus denitrificans distinct from thiamine phosphate phosphatase

J Biochem. 1977 Jul;82(1):307-9. doi: 10.1093/oxfordjournals.jbchem.a131686.

Abstract

To determine whether the acid phosphatase in Micrococcus denitrificans participates in hydrolysis of thiamine phosphate in the synthesis of thiamine pyrophosphate, acid phosphatase was purified 280-fold by conventional procedures, which removed thiamine phosphate phosphatase completely. Studies showed that this acid phosphatase is a different protein from thiamine phosphate phosphatase and that it has no binding site for thiamine phosphate on its active site.

MeSH terms

  • Acid Phosphatase / isolation & purification
  • Acid Phosphatase / metabolism*
  • Paracoccus denitrificans / enzymology*
  • Phosphoric Monoester Hydrolases / metabolism*
  • Thiamine / analogs & derivatives
  • Thiamine / metabolism
  • Thiamine Pyrophosphate / metabolism

Substances

  • thiamine monophosphatase
  • Acid Phosphatase
  • Phosphoric Monoester Hydrolases
  • Thiamine Pyrophosphate
  • Thiamine