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Table 2 Kinetic parameters derived from progress curves of initial BMCC hydrolysis: association (kon), catalytic (kcat), and dissociation (koff) rate constants, and apparent processivity number (n)

From: Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum

Enzyme kon (g−1 L s−1) kcat (s−1) koff (s−1) n
TreCel7A 0.0055 ± 0.0002 4 ± 0.2 0.0066 ± 0.0005 89 ± 5
TreCel7A_CD 0.0034 ± 0.0005 4.9 ± 0.7 0.0049 ± 0.0012 88 ± 5
ThaCel7A 0.0056 ± 0.0002 4.8 ± 0.4 0.0061 ± 0.0002 74 ± 1
TatCel7A 0.0071 ± 0.0001 8.3 ± 0.3 0.0071 ± 0.0001 97 ± 1
TatCel7A_CD 0.0044 ± 0 6.8 ± 0.3 0.0066 ± 0.0002 87 ± 3
  1. These parameters were derived for the 0–200 s pre-steady-state time interval. The substrate load was 3.3 g/L, and the enzyme concentration was 50 nM