6.2.1.26	ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA	-	
6.2.1.26	ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA	kinetic ordered bi uni uni bi ping-pong mechanism	
6.2.1.26	ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA	bi uni uni bi ping-pong kinetic mechanism	
6.2.1.26	ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA	the enzyme adopts an ordered bi uni uni bi ping-pong mechanism, which involves ATP as the first binding substrate and a large conformational change during the catalysis. In MenE catalysis, tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site create a new binding site for the carboxylate substrate. Analysis of the adenylation half-reaction in the domain alteration catalytic mechanism of the adenylateforming enzymes, open-closed conformational change in ATP configuration of the adenylation active site