Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Reaction

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 2 of 2
EC Number Reaction Commentary Reference
Show all pathways known for 4.1.3.3Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.3aceneuramate = N-acetyl-D-mannosamine + pyruvate mechanism 33315, 650651, 651103, 652833, 652991
Show all pathways known for 4.1.3.3Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.3aceneuramate = N-acetyl-D-mannosamine + pyruvate the enzyme catalyzes a Bi-Uni ordered condensation reaction in which pyruvate binds first to the enzyme to form a catalytically important Schiff base. Tyr137 acts as the proton donor to the aldehyde oxygen of ManNAc during the reaction, the activation barrier is dominated by carbon-carbon bond formation, and proton transfer from Tyr137 is required to obtain a stable Neu5Ac-Lys165 Schiff base complex. A triad of residues, Tyr137, Ser47, and Tyr110 from a neighboring subunit, are required to correctly position Tyr137 for its function 726551
Results 1 - 2 of 2