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. 2023 Nov 14;13(23):15417–15426. doi: 10.1021/acscatal.3c04026

Table 1. Kinetic Parameters of Wild-Type OvoATh2 and Its Mutants under Different Conditions.

enzyme substrates kcat, O2 [min–1] KM, l-His or l-His derivatives [μM] KM, l-Cys [μM] kcat/KM, l-His or l-His derivatives or l-Cys [min–1μM–1] % of coupling product from NMR analysis
wild-type l-His + l-Cys 589.0 ± 3.5 585.1 ± 28.0 278.6 ± 9.0 2.10 ± 0.09 ∼90%
wild-type l-Her + l-Cys 127.2 ± 1.5 61.9 ± 3.5 (1.86 ± 0.04) E3 66.9 ± 2.3 ∼50%
wild-type l-Cys 26.7 ± 0.4   (2.6 ± 0.2) E3   below the detection limit
wild-type 3-Me-l-His + l-Cys 131.2 ± 2.7 1.9 ± 0.1 252.2 ± 14.5 0.52 ± 0.04 below the detection limit
wild-type 1-Me-l-His + l-Cys 20.5 ± 0.3   (3.9 ± 0.1) E3 (5.3 ± 0.1) E-3 below the detection limit
enzyme substrates kcat, O2 [min–1] KM, l-His [μM] KM, l-Cys [μM] kcat/KM, l-Cys [min–1 μM–1] % of coupling product from NMR analysis
Y406F l-His + l-Cys 361.2 ± 5.9 38.2 ± 2.6 575.2 ± 22.0 0.63 ± 0.09 ∼20%
Y68F l-His + l-Cys 23.4 ± 0.2 50.9 ± 2.5 (61.9 ± 1.5) E3 (0.4 ± 0.1) E-3 ∼30%
Y68F/Y406F l-His + l-Cys 14.8 ± 0.3 31.3 ± 4.0 (125.7 ± 11.0) E3 (1.2 ± 0.1) E-4 ∼10%