The extracellular acid phosphatase of the mosquito-parasitizing fungus Lagenidium giganteum.
The mosquito-parasitizing fungus Lagenidium giganteum secreted a soluble acid phosphatase and beta-D-glucosidase into the growth medium. The acid phosphatase was isolated and purified to single component, and some of its physicochemical properties were determined. The enzyme exhibited a pH optimum of 5.6 in phthalate buffer with p-nitrophenyl phosphate and was temperature-inactivated at 55 degrees C. Enzyme activity seems to be limited to phenyl-phosphate substrates. A molecular weight of 42,800 was found and the amino acid content was also determined. A Km for p-nitrophenyl phosphate of 1.6 x 10(-7) M was found. The possible involvement of the enzyme in the infective process was discussed.
Bell
T J
TJ
Lee
B
B
Domnas
A J
AJ
D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D008411:Chytridiomycota / Q000201:enzymology*; D009033:Culicidae / Q000382:microbiology*; D007700:Kinetics; D009868:Oomycetes / Q000201:enzymology*; D013379:Substrate Specificity
D000596:Amino Acids; D000135:Acid Phosphatase