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. Author manuscript; available in PMC: 2017 May 24.
Published in final edited form as: Biochemistry. 2016 Nov 2;55(45):6295–6303. doi: 10.1021/acs.biochem.6b00928

Table 1.

Summary of MtIlvE Michaelis–Menten Constants in the Presence of Different α-Keto Acids and L-Glutamatea

substrate KM (×10−3 M) V (s−1) V/K (×104 M−1 s−1)
L-glutamate 1.30 ± 0.2 8.9 ± 0.4 0.7
α-keto-methyl-oxopentanoic acid 0.10 ± 0.01 6.2 ± 0.2 6.2
α-ketoisocaproate 0.24 ± 0.03 9.1 ± 0.4 3.8
α-ketoisovalerate 0.16 ± 0.01 5.9 ± 0.1 3.6
α-keto-phenylpyruvic acid 0.64 ± 0.1 1.4 ± 0.04 0.2
α-keto-γ-methylthiobutyric acid 6.07 ± 0.3 8.7 ± 0.1 0.2
a

V is the constant for the catalytic turnover of the enzyme. K is the substrate concentration necessary for the enzyme to reach half of its Vmax. V/K is the substrate specificity.