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. Author manuscript; available in PMC: 2008 Sep 15.
Published in final edited form as: Biochemistry. 2007 May 12;46(22):6536–6546. doi: 10.1021/bi6026506

Table 3.

Substrate Kinetics

Enzyme Substrate KM (µM) kcat (s−1) kcat/KM (µM−1 s−1) Relative Catalytic Eff.a
Wild-type Acetate 6047 ± 1024 276.8 ± 21.4 0.045 ± 0.008
Propionate 9413 ± 1709 261.0 ± 20.8 0.027 ± 0.005
Glycine 9450 ± 1658 259.4 ± 13.3 0.027 ± 0.005
V386A Acetate 6403 ± 701 183.5 ± 10.3 0.028 ± 0.003 0.6
Propionate 1539 ± 119 93.4 ± 2.4 0.060 ± 0.005 2.2
V310D Acetate 2464 ± 321 232.0 ± 12.3 0.090 ± 0.010 2.0
Glycine 8367 ± 753 165.5 ± 6.4 0.020 ± 0.002 0.7
a

Relative catalytic efficiency is defined as the ratio of kcat/KM for a particular substrate for the mutant enzyme compared to the wild-type.