Discovery of the 5-Chlorokynurenine Pathway in Lodopyridone Biosynthesis
CNQ490 marine actinobacterium. We characterized the enzymes responsible for the conversion of L-tryptophan to L-5-chlorokynurenine, including Lodo315, a tryptophan 2,3-dioxygenase (TDO) enzyme with extensive substrate flexibility. This work expands our current knowledge of TDO enzymes that act on halogenated tryptophan substrates in bacteria and serves as a future basis for bioproduction of chlorinated kynurenine scaffolds.
Authors
- Bradley S. Moore (ORCID: https://orcid.org/0000-0002-4652-1253)
- Tian Lan (ORCID: https://orcid.org/0000-0002-4099-5386)
- Mariah J. Avila (ORCID: https://orcid.org/0000-0001-7050-400X)
Institutions
- Scripps Institution of Oceanography (US)
- University of California San Diego (US)
Publication Details
- Journal
- Journal of Natural Products
- Published
- 2026-06-12
- DOI
- https://doi.org/10.1021/acs.jnatprod.6c00490
- Primary Topic
- Tryptophan and brain disorders
- Type
- article
- Field-Weighted Citation Impact
- 0.00