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Methylation is a phase II biotransformation process involving the attachment of a methyl group to a substrate. Enzymes known as methyltransferases orchestrate this reaction.
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Evidence for C-Methylation Proceeding via a Cyclopropane Intermediate during Tabtoxin Biosynthesis.

Ruihao Li1, Luting Fang1, Wei Wei1

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|April 24, 2026
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Researchers uncovered a novel C-methylation pathway in tabtoxin biosynthesis involving cyclopropane formation and hydrolysis. This discovery reveals a new branch of lysine biosynthesis and enzyme functions crucial for natural product synthesis.

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Area of Science:

  • Biochemistry
  • Natural Product Biosynthesis
  • Enzymology

Background:

  • Genomic era natural product discovery necessitates enzyme function validation.
  • Tabtoxin biosynthesis involves complex pathways for antimicrobial and herbicidal compounds.

Purpose of the Study:

  • Elucidate the biosynthetic logic of a rare C-methylation at the C5-position of lysine in tabtoxin.
  • Identify novel enzymes and pathways involved in tabtoxin precursor synthesis.

Main Methods:

  • Enzyme characterization of novel SAM-dependent cyclopropane synthase (TblA) and dual function cyclopropane hydrolase/N-acyltransferase (TabB).
  • Analysis of metabolic branching via TabD-catalyzed transamination on l-2,3,4,5-tetrahydro-dipicolinic acid (THDPA).

Main Results:

  • Established a novel biosynthetic pathway for C5-methylation involving cyclopropane ring formation and hydrolysis.
  • Identified TblA as a SAM-dependent cyclopropane synthase and TabB as a dual function enzyme.
  • Discovered a new metabolic branch of lysine biosynthesis providing direct access to meso-diaminopimelate via THDPA.

Conclusions:

  • The study elucidates the mechanistic basis and enzyme order for C1-unit incorporation in tabtoxin biosynthesis.
  • Findings explain the construction of monobactams in the tabtoxin family, expanding knowledge of natural product synthesis.