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. 1997 Aug 5;94(16):8491–8496. doi: 10.1073/pnas.94.16.8491

Table 1.

Kinetic parameters of wild-type and mutant chorismate mutases

Protein Value of protein with amino acid replacement
Inhibited (100 μM tyrosine)
Unliganded
Activated (10 μM tryptophan)
kcat, s−1 Km, S0.5, mM nH kcat/Km, mM−1⋅s−1 kcat, s−1 Km, S0.5, mM nH kcat/Km, mM−1⋅s−1 kcat, s−1 Km, S0.5, mM nH kcat/Km, mM−1⋅s−1
Wild type 387 11.8* 1.4 32.8 360 3.8 1.6 94.7 348 0.4 1.1 870.0
Asn194Asp 282 4.4 1.77 64.1 305 3.3 1.4 92.4 256 0.5 1.0 512.0
Glu246Gln 52 0.15 1.1 346.7 50 0.13 0.92 384.6 46 0.06 0.85 766.7

Values for kcat, Km, S0.5 were determined by fitting initial velocity data to equations describing hyperbolic or cooperative saturation, respectively. Hill coefficients (nH) were calculated from Hill plots by linear regression. 

*

Values resulted in uncertainty intervals >10% from the fitting procedure. 

Linear Eadie–Hofstee plots indicated hyperbolic saturation.