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Dynamic Lysine Acetylation Disrupts Isocitrate Lyase Function and Enables Metabolic Optimisation.

Adrián Martínez-Vivancos1,2, Beatriz Gomariz-Turpin1,2, Gema Lozano-Terol1,3

  • 1Department of Biochemistry and Molecular Biology (B) and Immunology, Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", Murcia, Spain.

Microbial Biotechnology
|March 30, 2026
PubMed
Summary

Acetylation of Escherichia coli isocitrate lyase (ICL) regulates its activity. Modifying specific sites (K13, K308) enhances metabolic flexibility and bioproduction, offering a new metabolic engineering strategy.

Keywords:
genetic code expansionglyoxylate cycleisocitrate lyaselysine acetylationpost‐translational modification

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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Area of Science:

  • Biochemistry
  • Microbial Metabolism
  • Enzyme Regulation

Background:

  • Proteomic studies indicate Escherichia coli isocitrate lyase (ICL) is acetylated, impacting its activity.
  • The precise molecular mechanisms and specific lysine residues involved in ICL acetylation were previously undefined.

Purpose of the Study:

  • To elucidate the molecular basis of ICL acetylation in E. coli.
  • To define the role of specific lysine residues in ICL regulation.
  • To explore the application of ICL regulation for metabolic engineering.

Main Methods:

  • Investigated acetyl-phosphate-dependent acetylation and CobB deacetylase reversibility.
  • Performed site-specific mutagenesis (K13R, K308R) to assess regulatory impact.
  • Engineered lysine-to-arginine substitutions directly into the chromosomal aceA gene.
  • Evaluated metabolic flux, biomass yield, and bioproduction (lycopene).

Main Results:

  • Acetylation at K13 and K308 inhibits ICL activity by destabilizing its tetrameric structure and promoting degradation.
  • Lysine-to-arginine substitutions at K13 and K308 enhance carbon flux, metabolic flexibility, and biomass yield.
  • A chromosomal KR mutant (aceA K13R/K308R) maintained growth rates, reduced acetate overflow, and improved metabolic balance.
  • This engineered strain achieved a 61% increase in lycopene production.

Conclusions:

  • ICL acetylation is a reversible post-translational regulatory mechanism within the glyoxylate shunt.
  • Targeted modification of ICL acetylation sites offers a powerful strategy for metabolic engineering.
  • This regulatory approach can optimize microbial cell factories for sustainable bioproduction of valuable compounds.