Isolation and properties of glucose-1-phosphatase from mycelia of Pholiota nameko.
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.
Joh
T
T
Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, Japan. joh@agr.niigata-u.ac.jp
Yazaki
J
J
Suzuki
K
K
Hayakawa
T
T
D001487:Basidiomycota / Q000201:enzymology* / Q000648:ultrastructure; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D029968:Escherichia coli Proteins; D008970:Molecular Weight; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification*; D013379:Substrate Specificity