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. 2021 Dec 2;12:7030. doi: 10.1038/s41467-021-27144-4

Table 1.

Enzyme kinetic parameters for the sugar transfer of OsUGT91C1 and the mutants.

Substrate Enzyme kcat (min−1) Km (μM) kcat/Km (s−1 M−1) Fold
Rubu WT 2.0 ± 0.1 49.5 ± 5.3 673 1
(Combined β (1–2) F208M 2.4 ± 0.1 20.9 ± 1.7 1914 2.8
at R1 and R2) H93W 1.3 ± 0.1 56.8 ± 8.5 381 0.6
F379A 2.7 ± 0.1 16.5 ± 2.8 2727 4.1
H93W/F208M 1.8 ± 0.1 43.6 ± 5.4 688 1.0
F379A/F208M 2.8 ± 0.1 11.7 ± 1.0 3989 5.9
S13G WT 2.9 ± 0.1 24.9 ± 2.5 1941 1
(β (1–2) at R1) F208M 3.9 ± 0.1 18.7 ± 1.7 3476 1.8
H93W 3.9 ± 0.1 36.2 ± 4.7 1796 0.9
F379A 5.8 ± 0.2 19.0 ± 2.6 5088 2.6
H93W/F208M 3.5 ± 0.1 29.1 ± 2.2 2005 1.0
F379A/F208M 3.5 ± 0.1 9.7 ± 1.9 6014 3.1
Reb A WT 1.22 ± 0.02 45.7 ± 3.0 445 1
(β (1–2) at R2) F208M 2.9 ± 0.1 25.2 ± 2.0 1918 4.3
H93W 0.60 ± 0.03 58 ± 12 172 0.4
F379A 1.16 ± 0.02 37.0 ± 2.5 523 1.2
H93W/F208M 2.05 ± 0.03 63.9 ± 3.6 535 1.2
F379A/F208M 1.7 ± 0.1 15.1 ± 2.6 1876 4.2
STB WT 0.63 ± 0.03 71 ± 12 148
(β (1–6) at R1) H93W ND
F379A ND
H93W/F208M ND
F379A/F208M ND

WT wild type, ND non-detectable, fold fold change over the kcat/Km of the wide type for each substrate.

Assays were performed as described in Methods section. Nonlinear fitting values ±SD (n = 3) are shown. Source data are provided as a Source Data file.