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Table 1 Enzyme kinetics parameters with pNP-Lac as substrate and inhibition constants for cellobiose, at pH 4.5 and 30 °C

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

Enzyme kcat (s−1) KM (mM) kcat/KM (s−1 M−1) Ki (µM)
TreCel7A_CD 0.057 0.72 79 24
TatCel7A_CD 0.019 1.00 19 72
ThaCel7A_CD 0.067 0.90 75 49
  1. Ki is the competitive inhibition constant with 100 µM cellobiose in the reactions. The RMSD between calculated and experimental reaction rates was 3.4, 4.0, and 2.4% for TreCel7A_CD, TatCel7A_CD, and ThaCel7A_CD, respectively