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EC Number Inhibitors Commentary Structure
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39phosphoenolpyruvate - Go to the Ligand Summary Page
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39phosphoenolpyruvate activates at low concentrations, deactivation at high concentrations Go to the Ligand Summary Page
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39pyruvate - Go to the Ligand Summary Page
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39pyruvate product inhibition Go to the Ligand Summary Page
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39pyruvate isozyme NAD-ME2, uncompetitive versus NAD+, mixed inhibition versus (S)-malate. Pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q; pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q Go to the Ligand Summary Page
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39Tartrate - Go to the Ligand Summary Page
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39Tartrate substrate analogue, isozyme NAD-ME2, uncompetitive versus NAD+, competitive versus (S)-malate Go to the Ligand Summary Page
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39Tartronate - Go to the Ligand Summary Page
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39Tartronate binding site structure at the active site, competitive Go to the Ligand Summary Page
Show all pathways known for 1.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.39Urea denaturation, in 3-5 M urea, the enzyme undergoes a reversible tetramer-dimer-monomer quaternary structural change in an acidic pH environment, which resulted in a molten globule state that is prone to aggregate, Mn2+ protects, overview Go to the Ligand Summary Page
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