title: Purification and properties of an acid phosphatase of Micrococcus denitrificans distinct from thiamine phosphate phosphatase.
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: D000135:Acid Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D010231:Paracoccus denitrificans / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D013831:Thiamine / Q000031:analogs & derivatives / Q000378:metabolism; D013835:Thiamine Pyrophosphate / Q000378:metabolism
chemical_list: C022734:thiamine monophosphatase; D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases; D013835:Thiamine Pyrophosphate; D013831:Thiamine