. 2009 Dec 1;40(4):795–807. doi: 10.1590/S1517-838220090004000010

Table 4.

Kinetic constants for enzymatic myo-inositol trisphosphate dephosphorylation

phytase	InsP3 generated by
kinetic constant	Aspergillus niger phytase	S. cerevisiae phytase
Aspergillus niger	K_M [μmol l^-1]	215 ± 11^a	223 ± 14^a
	k_cat [s^-1]	101 ± 9^a	106 ± 11^a
S. cerevisae	K_M [μmol l^-1]	284 ± 15^a	293 ± 12^a
	k_cat [s^-1]	96 ± 7^a	99 ± 9^a

Temperature: 37°C; buffer: 100 mM sodium acetate, pH 5.0; enzyme concentration: 25 mU ml^-1. For calculation of kcat the following molecular masses were used: Aspergillus niger, 85 kDa, Saccharomyces cerevisiae, 60 kDa (12). The data are mean values of five independent experiments.

means within the same line with the same superscripts are not significantly different (P < 0.05)