| Abstract
| - The mechanism of N-methyltryptophan oxidase, a flavin-dependent amine oxidase fromEscherichia coli, was studied using a combination of kinetic isotope effects and theoretical calculations.The 15(kcat/Km) kinetic isotope effect for sarcosine oxidation is pH-dependent with a limiting value of0.994−0.995 at high pH. Density functional theory calculations on model systems were used to interpretthese isotope effects. The isotope effects are inconsistent with proposed mechanisms involving covalentamine-flavin adducts but cannot by themselves conclusively distinguish between some discrete electron-transfer mechanisms and a direct hydride-transfer mechanism, although the latter mechanism is moreconsistent with the energetics of the reaction.
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