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. 2014 Apr 15;9(4):e95170. doi: 10.1371/journal.pone.0095170

Table 1. Kinetic parameters and substrate inhibition of CtCBM22A_GOOOX-VN on cello-oligosaccharides and xylo-oligosaccharides.

Kinetic parameters* Substrate inhibition
k cat (min−1) K m (mM) k cat/K m (mM−1 min−1) V i/V max (%) K i (mM) n H **
Glucose 1,090 ± 16 11 ± 1 95 ± 7
Cellobiose 1,148 ± 5 0.060 ± 0.001 19,300 ± 300 45 2.9 ± 0.3 1.3
Cellotriose 1,210 ± 60 0.09 ± 0.01 12,800 ± 1,900 50 1.88 ± 0.16 1.5
Cellopentaose 1,080 ± 30 0.08 ± 0.01 14,100 ± 1,800 56 2.2 ± 0.3 1.5
Cellohexaose 1,190 ± 40 0.13 ± 0.01 9,000 ± 1,000 62 1.4 ± 0.3 1.3
Xylose 1,230 ± 20 135 ± 8 9 ± 1
Xylobiose 1,350 ± 30 0.09 ± 0.01 14,500 ± 1,400 75 8 ± 2 1.5
Xylotriose 1,330 ± 30 0.12 ± 0.01 11,000 ± 1,000 71 6 ± 3 1.2
Xylopentaose 1,630 ± 50 0.10± 0.01 15,700 ± 1,900
Xylohexaose 1,340 ± 40 0.12 ± 0.02 11,500 ± 1,600

*Data are mean values ± standard errors; 16 nM of enzyme was used in each reaction.

**Hill coefficient, values greater that one indicate positive cooperative binding.

– No inhibition detected with used substrate concentrations.