5.4.99.5	additional information	-	Chorismic acid	Competetive inhibition by I – IV Structur: increase the Km	672622	
5.4.99.5	additional information	-	additional information	A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol)	674312	
5.4.99.5	additional information	-	additional information	due to instability of chorismate at higher temperature, a Km value is not determined	692260	
5.4.99.5	additional information	-	additional information	Michaelis-Menten kinetics	747259, 749355	
5.4.99.5	additional information	-	additional information	Michaelis-Menten steady-state kinetics	747032	
5.4.99.5	additional information	-	additional information	sigmoid substrate saturation curve with S0.5: 16.7 mM for chorismate at 37°C and S0.5: 12 mM for chorismate at 37°C in presence of 0.1 mM tyrosine	651660	
5.4.99.5	additional information	-	additional information	steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview	748178	
5.4.99.5	additional information	-	additional information	steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics	748178	
5.4.99.5	additional information	-	additional information	steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site	748178	
5.4.99.5	additional information	-	additional information	The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown	672268