Isolation and properties of glucose-1-phosphatase from mycelia of Pholiota nameko

Biosci Biotechnol Biochem. 1998 Nov;62(11):2251-3. doi: 10.1271/bbb.62.2251.


An acid phosphatase with a very high substrate specificity for glucose-1-phosphate was isolated for the first time from mycelia of Pholiota nameko. The molecular weight of the enzyme was estimated to be 31,000 on gel filtration and 35,000 on SDS-PAGE. The activity was inhibited by Cu2+, Hg2+, molybdate, and tartaric acid. The sequence of N-terminal 20 amino acid residues was analyzed.

MeSH terms

  • Basidiomycota / enzymology*
  • Basidiomycota / ultrastructure
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli Proteins*
  • Molecular Weight
  • Phosphoric Monoester Hydrolases / isolation & purification*
  • Substrate Specificity


  • Escherichia coli Proteins
  • agp protein, E coli
  • Phosphoric Monoester Hydrolases