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. Author manuscript; available in PMC: 2009 Dec 18.
Published in final edited form as: Biochemistry. 2009 Sep 22;48(37):8869–8878. doi: 10.1021/bi900968a

Table 1.

Kinetic Properties of Wild-Type and Mutant Forms of IDH

isocitratea
NAD+b
enzyme Vmax (U/mg) (−AMP/+AMP) S0.5 (mM) (−AMP/+AMP) Hill coef. (−AMP/+ AMP) Vmax(U/mg) S0.5 (mM)
wild-type 30.5/31.8 (±1.0/1.6) 0.57/0.10 (±0.04/0.01) 3.6/3.5 (±0.1/0.3) 35.0 0.12
C56S/C242S 29.8/31.7 (±1.5/2.1) 1.11/0.16 (±0.02/0.04) 3.6/3.1 (±0.1/0) 30.7 0.08
C150S 38.7/40.3 (±1.4/2.5) 0.85/0.19 (±0.01/0.02) 2.5/2.5 (±0.4/0.3) 39.9 0.10
a

Kinetic properties were determined as described under Experimental Procedures. Properties with respect to isocitrate were determined in the absence or presence of 100μM AMP, and values represent three independent measurements (±standard deviations).

b

Values for kinetic properties with respect to NAD+ represent averages of two independent measurements.