The transamination of L-tryptophan by streptomyces flocculus was carried out in deuterated buffer to provide information on the mechanism of this enzyme catalyzed reaction. A number of mechanisms can be proposed for the transamination reaction. The simplest mechanism is the classical aldimine formation with pyridoxal phosphate, prototropic shift of the new imine to 3-indole pyruvic acid. Reamination is thought to be the reverse process. Mass spectrometric fragmentation patterns were used to determine the position of hydrogen-deuterium exchange, and thus which mechanistic pathway the transamination followed.
|Original language||English (US)|
|Number of pages||2|
|Journal||Annual Conference on Mass Spectrometry and Allied Topics|
|State||Published - Dec 1 1984|