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. 2012 Oct;78(20):7223–7228. doi: 10.1128/AEM.01366-12

Table 3.

Kinetic parameters of WT and Y172A CgAM enzymes derived from the disproportionation reaction using maltotriose as the substratea

CgAM enzyme Km (mM) kcat (min−1 [103]) kcat/Km (mM−1min−1 [103])
Wild type 19.6 ± 3.2 9.37 ± 1.1 0.479 ± 0.1
Y172A mutated 12.9 ± 0.8 2.17 ± 0.2 0.168 ± 0.1
a

Data shown are the mean ± standard deviation and are derived from Lineweaver-Burk plots of the results of three independent sets of different enzyme-substrate concentrations with product analysis at different time points.