The glycosylated human MINPP (multiple inositol polyphosphate phosphatase), which was recombinantly over-expressed by using industrial host, Pichia pastoris, showed the phytase activity against phytate (InsP6) and the enzyme activity of the unglycosylated counterpart was decreased to 30%. The optimal phytase activity occurred at pH 7.4. The human MINPP showed high substrate specificity for InsP6 with little activity on other organic phosphate conjugates such as para-nitrophenylphosphate (pNPP), ATP, and ribose-1-phosphate (R-1-P). The phosphatase activity against 2,3-bisphosphoglycerate (2,3-BPG) by human MINPP was increased to 1.2-fold in the presence of stimulator, 1 mM 2-phosphoglycolate (2-PG) but the phytase activity against InsP6 was not affected by addition of 1 mM 2-PG. The phosphatase activity against 2,3-BPG by human MINPP was not increased in the presence of 2 mM Mg 2+ or 100 mM Cl -.
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