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. Author manuscript; available in PMC: 2011 Jun 15.
Published in final edited form as: Arch Biochem Biophys. 2010 Apr 22;498(2):83–88. doi: 10.1016/j.abb.2010.04.015

Table 1.

Steady-state kinetic parameters for wild type and K315M PAO

pH 8 pH 10

enzyme kcat/KO2 (mM−1 s−1) KO2 (mM) kcat (s−1) kcat/KO2 (mM−1 s−1) KO2 (mM) kcat (s−1)
Wild-type 14 ± 1 0.32 ± 0.05 4.3 ± 0.2 21 ± 3 0.99 ± 0.25 20.5 ± 2.6
K315M 1.2 ± 0.1 1.0 ± 0.1 1.2 ± 0.1 0.7 ± 0.1 6 ± 6 4 ± 4

*Conditions: 1 mM N1-acetylspermine, 0.05 mM Tris-HCl (pH 8) or CAPS (pH 10), 20° C