Extended Data Fig. 3: Kinetics of the SAcBesB reaction.
From: Terminal alkyne formation by a pyridoxal phosphate-dependent enzyme
Steady state kinetic analysis of BesB with respect to its substrate 4-chloroallylglycine (1). Each chosen concentration (20 μM to 2 mM) of 1 was performed in triplicate. Data points were subjected to non-linear curve fitting to Michaelis-Menten equation to obtain the kinetic parameters kcat = 0.0228 ± 0.0003 s-1, KM = 47 ± 3 μM.
