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EC Number Reaction Commentary Reference
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ - -
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ acid-base chemical mechanism for Ascaris suum malic enzyme 685215
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ active site structure, catalytic residues are Y126, R181, K199, D295, N343, and N479 654651
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ catalytic mechanism, malate is bound deeply in the active site, Mn2+ catalyzes the entire reaction, Lys183 is the general base for oxidation, Tyr112-Lys183 functions as the general acid-base pair to catalyze the tautomerization of the enolpyruvate product from decarboxylation to pyruvate, substrate and cofacor binding modes 657362
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ isozyme NAD-ME2 and chimeric mutant NAD-ME1q follow a sequential ordered Bi-Ter mechanism, NAD+ being the leading substrate followed by (S)-malate. Hetereodimer NAD-MEH can bind both substrates randomly. Interaction between NAD-ME1 and -ME2 generates a heteromeric isozyme NAD-MEH with a particular kinetic behaviour 711147
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ isozyme NAD-ME2 and chimeric mutant NAD-ME1q follow a sequential ordered Bi-Ter mechanism, NAD+ being the leading substrate followed by (S)-malate. Isozyme NAD-ME1 and hetereodimer NAD-MEH can bind both substrates randomly. However, NAD-ME1 shows a preferred route that involves the addition of NAD+ first. interaction between NAD-ME1 and -ME2 generates a heteromeric isozyme NAD-MEH with a particular kinetic behaviour 711147
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ rapid equilibrium reaction of the intersecting type 286711
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ reaction mechanism of oxidative decarboxylation 654623
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ reaction mechanism, active site structure, enzyme-cofactor interactions, overview 656163
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ sequential mechanism 286707
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