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Results 1 - 10 of 17 > >>
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EC Number Inhibitors Commentary Structure
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210more inactivation of the enzyme following modification of carboxyl and imidazole moieties is a consequence of a loss in substrate binding and catalysis in the glucosyltransfer reaction. No inhibition by serine modifiying diisopropyl fluorophosphate and cysteine modifying 4-chloromercuribenzoate and iodoacetamide Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210Mg2+ 10 mM, 22% inhibition Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210Ca2+ 10 mM, 13% inhibition Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210Cu2+ 5 mM, 58% inhibition Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210Cu2+ - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210EDTA 1 mM, complete inactivation Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210Hg2+ 1 mM, 33% inhibition Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210Hg2+ - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210N-bromosuccinimide modifies tryptophan residues and inactivates the enzyme, loss of LGTase activity by NBS treatment is partially protected by pre-incubating the enzyme with excess limonin Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.210diethyldicarbonate modifies histidine residues and inactivates the enzyme, pseudo first order kinetics. When the histidine modification is reversed by hydroxylamine treatment, 79% of the activity is restored Go to the Ligand Summary Page
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