2.3.1.20	additional information	-	additional information	-	486497	
2.3.1.20	additional information	-	additional information	acyl-CoA substrate binding kinetics of the recombinant N-terminal fragment, overview	672791	
2.3.1.20	additional information	-	additional information	isozyme BnaC.DGAT1.a exhibits positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. Kinetics of wild-type and enzyme mutants, Michaelis-Menten kinetic model	758047	
2.3.1.20	additional information	-	additional information	kinetic analysis of lipidated BnaDGAT1. BnaDGAT1 exhibits cooperative substrate binding behavior with oleoyl-CoA	758018	
2.3.1.20	additional information	-	additional information	kinetics of wax synthase activity, overview	756245	
2.3.1.20	additional information	-	additional information	Michaelis-Menten kinetics	757051, 757183	
2.3.1.20	additional information	-	additional information	Michaelis-Menten or allosteric sigmoidal kinetics	757545	
2.3.1.20	additional information	-	additional information	the flux control coefficient is 0.12 in oil palm	673535	
2.3.1.20	additional information	-	additional information	the flux control coefficient is 0.74 in olive	673535	
2.3.1.20	additional information	-	additional information	the N-terminal regions of Brassica napus DGAT1 enzymes binds acyl-CoA in a sigmoidal fashion, suggesting positive cooperative binding	757544