| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5287225 | Tetrahedron Letters | 2007 | 4 Pages |
Abstract
Indole-3-pyruvic acid is transformed to prodeoxyviolacein by the novel enzyme VioE, which is involved in the violacein biosynthetic pathway in Chromobacterium violaceum ATCC12472. VioE catalyzes the decarboxylation and indole-ring rearrangement of a nascent compound that is produced from indole-3-pyruvic acid and NH4+ by the action of chromopyrrolic acid synthase (VioB or StaD), and ultimately the reaction yields prodeoxyviolacein.
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Authors
Shumpei Asamizu, Yasuo Kato, Yasuhiro Igarashi, Hiroyasu Onaka,