Table 4. Kinetic constants of B. coagulans and B. clausii LMCOs compared to previously characterised B. pumilus CotA²⁸. Enzyme assays were carried out at the optimal pH for each substrate. Parameters were estimated with a Michaelis Menten equation with uncompetitive substrate inhibition.

		B. coagulans	B. clausii	B. pumilus28
ABTS	KM [μM]	31 ±3	132 ±11	80 ±4
	kcat [s−1]	69 ±3.1	90 ±2.3	291 ±2.7
	Ki [mM]	0.94 ±0.11	44 ±2.3	−
2,6-DMP	KM [μM]	628 ±67	8535 ±2394	680 ±27
	kcat [s−1]	17 ±0.8	65 ±15.2	11 ±0.1
	Ki [mM]	36 ±9.8	3.8 ±1.2	−