Abstract
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) |
|---|---|
| Pages (from-to) | 763-764 |
| Number of pages | 2 |
| Journal | Annual Conference on Mass Spectrometry and Allied Topics |
| State | Published - Dec 1 1984 |