Defluorination of 4-fluorothreonine by threonine deaminase

Linrui Wu, Hai Deng* (Corresponding Author)

*Corresponding author for this work

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)6236-6240
Number of pages5
JournalOrganic & Biomolecular Chemistry
Volume18
Issue number32
Early online date24 Jul 2020
DOIs
Publication statusPublished - 28 Aug 2020

Keywords

  • STREPTOMYCES SP MA37
  • AMINO-ACID OXIDASE
  • FLUOROMETABOLITE BIOSYNTHESIS
  • CRYSTAL-STRUCTURE
  • SNAKE-VENOM
  • IDENTIFICATION
  • PRODUCER

Fingerprint Dive into the research topics of 'Defluorination of 4-fluorothreonine by threonine deaminase'. Together they form a unique fingerprint.

  • Cite this