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. 2023 May 15;62(11):1807–1822. doi: 10.1021/acs.biochem.3c00150

Table 2. Summary of Apparent Kinetic Parameters Determined for the Wild-Type and Variant Enzymes Studied in This Work.

enzyme and substrate KMapp (μM) kcatapp (min–1) kcatapp/KMapp (M–1 s–1)
TsaM, VanB, and vanillate 182 ± 3.7 1.8 ± 0.7 230 ± 48
TsaM variant 14, VanB, and vanillate 13 ± 0.8 3.8 ± 0.2 5100 ± 530
TsaM variant 15, VanB, and vanillate 20 ± 1.2 3.7 ± 0.2 3200 ± 260
VanA, VanB, and vanillate 6.4 ± 0.6 3.4 ± 0.3 8900 ± 800
TsaM, VanB, and dicamba N/A N/A N/A
TsaM variant 15, VanB, and dicamba 100 ± 9.2 1.8 ± 0.2 300 ± 43
TsaM variant 18, VanB, and dicamba 42 ± 6.2 2.8 ± 0.3 1100 ± 200
TsaM variant 18, DdmA, DdmB, and dicamba 39 ± 7.2 2.7 ± 0.2 1200 ± 240
DdmC, DdmA, DdmB, and dicamba 28 ± 3.4 2.8 ± 0.1 2100 ± 240
DdmC, VanB, and dicamba 22 ± 4.1 2.8 ± 0.3 2300 ± 410