Comparison of the phosphate-repressible and-constitutive acid phosphatases of Yarrowia lipolytica.

The phosphate-repressible acid phosphatase from Yarrowia lipolytica cells was more thermostable but more sensitive to urea denaturation and to the effect of Triton X-100 than the constitutive counterpart. The K m values of the repressible and constitutive enzymes for p-nitrophenyl phosphate were 3.6 mM and 7.4 mM, respectively. They are judged to be distinct proteins.