What are kinetics values mentioned in this excerpt? Please mention kcat and kM values for each enzyme-substrate pair. 
Please format your results like this: 
```
PAIR: <enzyme>, <substrate>
KCAT: <kcat>
KM: <kM>
INFO: <extra info, as needed>
```
Here is the excerpt.
## RESULTS

The inhibition activity of soybean lipoxygenase-1 was measured by two methods for comparison, because this enzyme seems to be sensitive to assay conditions. Soybean lipoxyge- nase-1 is known to catalyze the dioxygenation of the ( Z , Z )- diene moiety of linoleic acid. In plants, the primary dioxygen- ation product is 13 S linoleic acid hydroperoxide (13-HPOD) ( 1 ). Hence, the enzyme assay was usually performed using a UV spectrophotometer to detect the increase at 234 nm associated with the ( Z , E )-conjugated double bonds newly formed in the product but not the substrate. In many previous studies, the data were usually obtained at pH 9 because soybean lipoxygenase-1 is reported to have its optimum at pH 9.0 ( 12 ), but the absorption at 234 nm suffered from unstable baseline activity of unknown origin attributable to the presence of octyl gallate at pH 9.0. This pseudoactivity of the blank control had to be subtracted from activity of the enzyme assay, making precise measurements difficult. Moreover, this basic pH value may not be practical to use for food protection. Because the stable data were obtained at pH 8.0, the evaluation was performed at pH 8.0 ( 10 ). The data obtained were also compared with those of NDGA used as a reference compound. Its IC50was obtained as 82 Âµ M when the experiment was performed at pH 9.0 but 0.2 Âµ M at pH 8.0. As a result, octyl gallate showed a dose-dependent inhibitory effect on this oxidation as shown in Figure 2 . As octyl gallate increased, the enzyme activity was rapidly decreased but not completely suppressed. The IC50 was estimated to be 1.3 Âµ M. As the need arose, the assay was also monitored by using polarography (oxygen consumption) for comparison. The IC50 obtained was 2.1 Âµ M, which is almost comparable with that measured by using the spectrophotometric method. The oxidation of linoleic acid catalyzed by soybean lipoxy- genase-1 follows Michaelis - Menten equations. The plots of the remaining enzyme activity versus the concentrations of enzyme at different concentrations of octyl gallate gave a family of straight lines, which passed through the origin as shown in Figure 3 . Increasing the inhibitor concentration resulted in descending slopes of the lines, indicating that the inhibition of