Skip to main content
. 2022 Sep 6;290(2):379–399. doi: 10.1111/febs.16602

Table 2.

Dissociation constants for oNPC and cellobiose binding to TrCel7A WT and catalytic mutants and PcCel7D from fluorescence titration experiments, and inhibition constants for cellobiose a and lactose.

Enzyme K d for oNPC (μm) K d for cellobiose (μm) K i for cellobiose a m) K i for lactose (μm) b
TrCel7A WT 7.4 ± 0.4 23 ± 4 24 c 180 ± 16
TrCel7A D214N 7.1 ± 0.7 8.9 ± 1.1
TrCel7A E212Q 4.7 ± 0.4 8.1 ± 0.3
TrCel7A E217Q 3.9 ± 0.4 14 ± 3
PcCel7D 110 ± 10 180 d 183 ± 16
a

Previously published inhibition constants from [13]

b

The error margin represents the 95% confidence interval of the profile likelihood from graphpad prism 8

c

Competitive inhibition constant from inhibition experiments with pNPL as substrate at 30 °C, pH 5.0 [13]

d

Mixed‐type inhibition constant (α = 5.7) estimated from inhibition experiments with CNP‐Lac (2‐chloro‐4‐nitrophenyl‐β‐lactoside) as substrate at 33 °C, pH 5.5 [13].