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. Author manuscript; available in PMC: 2010 Aug 1.
Published in final edited form as: Nat Struct Mol Biol. 2010 Jan 10;17(2):159–164. doi: 10.1038/nsmb.1737

Table 4.

Esterase Activity Activation Constants for ALDH2 and ALDH2*2a

Constant ALDH2 ALDH2 (0.5 mM NAD+) ALDH2*2 ALDH2*2 (1. 0 mM NAD+) ALDH2*2 (50 μM Alda-1)
Vo (min−1) 24.9 +/− 2.0 96.3 +/− 2.2 0.40 +/− 0.03 1.36 +/− 0.28 0.64 +/− 0.19
Vmax (min−1) 181 +/− 6.8 248 +/− 22 2.3 +/− 0.2 14.7 +/− 1.3 49.5 +/− 4.3
KAct(app) (μM) 3.4 +/− 0.5 2.6 +/− 0.1 16.1 +/− 5.8 11.2 +/− 1.3 2,820 +/− 330
Vmax (min−1) -- 242 +/− 14 -- -- --
Ki(app) (μM) -- 328 +/− 24 -- -- --
a

Data were fit to the non-essential activator expression (see Methods), where Vo is the initial velocity for the reaction in the absence of activator, Vmax is the maximal velocity and KAct is the concentration of activator required for half-maximal activation and Ki is the concentration required for half-maximal inhibition.