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Results 1 - 4 of 4
EC Number Reaction Commentary Reference
Show all pathways known for 6.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.26ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA - -
Show all pathways known for 6.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.26ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA bi uni uni bi ping-pong kinetic mechanism 727306
Show all pathways known for 6.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.26ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA kinetic ordered bi uni uni bi ping-pong mechanism 690915
Show all pathways known for 6.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.26ATP + 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 -, 745330
Results 1 - 4 of 4