Abstract
4-Fluorothreonine (4-FT) is the only naturally occurring fluorinated amino acid antibiotic. Although two conserved proteins in the 4-FT pathway have been found to be involved in self-detoxification mechanisms, the 4-FT-producing strains may also require an alternative pathway to degrade the intracellular 4-FT. In this study, we examined the possible degradation role of three enzymes involved in threonine metabolite pathways toward 4-FT as a possible degradation route to avoid in vivo 4-FT accumulation. Among these three enzymes, threonine deaminase was found to catalyse a defluorination reaction to generate 4-hydroxy-α-ketobutyrate, which is supposed to be further metabolised by an aldolase that likely is a unique occurrence in the 4-FT-producing strains. Our finding may constitute a 4-FT degradation pathway as a complementary resistance mechanism.
Original language | English |
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Pages (from-to) | 6236-6240 |
Number of pages | 5 |
Journal | Organic & Biomolecular Chemistry |
Volume | 18 |
Issue number | 32 |
Early online date | 24 Jul 2020 |
DOIs | |
Publication status | Published - 28 Aug 2020 |
Bibliographical note
Open Access via the Jisc RSC AgreementKeywords
- STREPTOMYCES SP MA37
- AMINO-ACID OXIDASE
- FLUOROMETABOLITE BIOSYNTHESIS
- CRYSTAL-STRUCTURE
- SNAKE-VENOM
- IDENTIFICATION
- PRODUCER