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Results 1 - 6 of 6
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EC Number Cofactor Commentary Reference
Display the reaction diagram Show all sequences 1.14.13.114FAD - 744353, 764159
Display the reaction diagram Show all sequences 1.14.13.114FAD NicC FAD binding site structure, overview 744353
Display the reaction diagram Show all sequences 1.14.13.114FAD the enzyme activity is NADH-dependent and FAD-dependent. The holoenzyme contains 1 M of FAD per 1 M of enzyme. FAD gradually dissociates from the enzyme during purification. Without FAD, no pure enzyme activity is observed, but after the addition of FAD, the apoenzyme is activated immediately 697700
Display the reaction diagram Show all sequences 1.14.13.114more riboflavin or FMN do not serve as enzyme cofactors 697700
Display the reaction diagram Show all sequences 1.14.13.114NADH - 700940, 744353, 764159
Display the reaction diagram Show all sequences 1.14.13.114NADH the enzyme activity is NADH-dependent and FAD-dependent. NADH is 5times more effective than NADPH 697700
Results 1 - 6 of 6
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