2.7.2.1	additional information	-	additional information	assay methods for both directions of reaction	659856	
2.7.2.1	additional information	-	additional information	lower Km of the Thermotoga maritima acetate kinase for acetate measured than that determined by earlier assay methods	691204	
2.7.2.1	additional information	-	additional information	Michaelis-Menten kinetics	738717	
2.7.2.1	additional information	-	additional information	Michaelis-Menten kinetics, kinetic analysis and mechanism, detailed overview	739218	
2.7.2.1	additional information	-	additional information	Michaelis-Menten kinetics, thermodynamics	739591	
2.7.2.1	additional information	-	additional information	the dependence of the activity on acetate and acetyl phosphate concentrations obeys the Michaelis-Menten kinetics, whereas the dependence on ATP and ADP concentrations is sigmoidal	737465	
2.7.2.1	additional information	-	additional information	the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics	738528	
2.7.2.1	0.0026	-	acetyl phosphate	carried out at various temperatures	642183	
2.7.2.1	0.016	-	ATP	mutant R91A, pH 7.0	659446	
2.7.2.1	0.0222	-	acetyl phosphate	at pH 8.0 and 37°C	757471