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EC Number Protein Variants Commentary Reference
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4C374A mutation of surface cysteine 374 to alanine alters substrate turnover and inactivation by cyclopropylamines 672525
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4C397A expressed protein catalytically inactive 394582
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4C397H expressed protein catalytically inactive 394582
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4C406A MAO-A, Km for serotonin and tyramine not altered 394587
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4D123A 2.4fold increase in Km-value for phenylethylamine, 3.3fold increase in IC50-value for clorgyline, 3.3fold increase in IC50-value for deprenyl 656047
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4D132A 2.2fold increase in Km-value for serotonin,1.8fold increase in IC50-value for clorgyline, 3.9fold increase in IC50-value for deprenyl 656047
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4E142K a MAOB mutant 702228
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4I199A mutant of MAO-B, shows reduced inhibition by (E)-5-styrylisatin and (E)-6-styrylisatin compared to wild-type MAO-B 702565
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4I199A the mutant exhibits catalytic properties with 4fold increased amine Km but unaltered kcat values 724966
Show all pathways known for 1.4.3.4Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.4I199A/Y326A the mutant exhibits catalytic properties with 75fold increased amine Km but unaltered kcat values. The mutant shows inhibitor binding properties more similar to those of isoform MAO A than to isoform MAO B. Benzylamine is a poor substrate for the double mutant 724966
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