Skip to main content
. 2005 Dec;71(12):8881–8887. doi: 10.1128/AEM.71.12.8881-8887.2005

TABLE 1.

Substrate specificity of native GOOX

Substrate Relative activitya
Kmb (mM) kcat (min−1) kcat/Km (mM−1 min−1)
0.2 mM maltose 10 mM maltose
Glucose 0.2 3.5 8.12 ± 0.16 546 ± 16 67
Lactose 6.4 3.8 0.066 ± 0.008 819 ± 25 12,400
Maltose 1.0 6.0 2.47 ± 0.05 531 ± 16 215
Maltotriose 1.1 6.2 1.11 ± 0.02 385 ± 12 348
Maltotetraose 0.4 4.3 2.51 ± 0.05 388 ± 12 155
Maltopentaose 0.2 2.6 10.6 ± 0.12 618 ± 18 58
Maltohexaose 0.2 3.1 2.60 ± 0.05 276 ± 11 106
Maltoheptaose 0.2 2.3 6.95 ± 0.15 415 ± 13 60
Cellobiose 7.7 2.8 0.048 ± 0.08 322 ± 11 6,710
Cellotriose 7.4 2.1 0.026 ± 0.002 776 ± 16 29,800
Cellotetraose 7.5 2.0 0.012 ± 0.002 200 ± 10 16,700
Cellopentaose 7.6 1.3 0.026 ± 0.003 239 ± 11 9,190
Cellohexaose 7.2 1.1 0.069 ± 0.007 222 ± 10 3,220
a

The enzyme activity with 0.2 mM maltose was defined as 1.

b

The kinetic parameter data are means ± standard errors for three independent experiments.