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. Author manuscript; available in PMC: 2007 Jun 15.
Published in final edited form as: J Biotechnol. 2006 Jun 6;126(2):248–259. doi: 10.1016/j.jbiotec.2006.04.028

Table 1.

InsP6 phosphatase (phytase) activity of MINPP

Enzyme Km (μM) Vmax (nmol/mg/min)
W.T. avian MINPP 140 ± 12 715 ± 31
Q78A avian MINPP 60 ± 2 625 ± 13
T27G avian MINPP 92 ± 2 30 ± 0.4
W.T. human MINPP 90 ± 1 6.2 ± 0.4

The kinetic parameters are for the hydrolysis of Mg–InsP6. These data were determined as described in Section 2. Most previous studies have used Na–InsP6 as a substrate. Thus, for comparative purposes, we determined the kinetic parameters of wild-type enzyme against Na–InsP6: the Km value was 200 ± 6 μM. The Vmax value was 501 ± 14 nmol/mg/min. All data represent means and standard errors from four experiments.