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Protein-Protein Complex Stability Controls Substrate Scope in a β-Ketoacyl-ACP Reductase Specific for Medium Chains.

Samuel J Andrzejewski1, Anika J Friedman1, Kathryn Mains1

  • 1Department of Chemical and Biological Engineering, University of Colorado, Boulder, 3415 Colorado Avenue, Boulder, CO, 80303, USA.

Angewandte Chemie (International Ed. in English)
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Summary
This summary is machine-generated.

Enzyme-acyl carrier protein (ACP) interactions control substrate specificity in metabolic pathways. Stabilizing these interactions enhances medium-chain preference, enabling control over fatty acid synthesis for metabolic engineering.

Keywords:
Assembly‐line enzymesBiocatalysisEnzymologyFatty acid synthesisMolecular recognition

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Metabolic Engineering

Background:

  • Assembly-line enzymes synthesize metabolites using acyl carrier proteins (ACPs) to shuttle intermediates.
  • Controlling enzyme reaction order is crucial for metabolic engineering but remains poorly understood.

Purpose of the Study:

  • Investigate the molecular basis of substrate specificity in β-ketoacyl-ACP reductase (PpFabG4).
  • Explore how enzyme-ACP interactions influence substrate selection in fatty acid synthesis.

Main Methods:

  • X-ray crystallography to analyze enzyme structure.
  • Molecular simulations to study enzyme-ACP interactions.
  • Site-directed mutagenesis to assess the impact of interaction strength on substrate specificity.

Main Results:

  • PpFabG4 exhibits unusual medium-chain selectivity, not explained by active site accessibility.
  • Substrate preference is dictated by the stability of the enzyme-ACP interaction, which is enhanced by medium acyl chains.
  • Mutational studies demonstrated over 100-fold changes in short-chain substrate activity by altering enzyme-ACP interaction strength.

Conclusions:

  • Enzyme-ACP interaction stability is a key determinant of substrate scope in promiscuous enzymes.
  • Findings provide a mechanism for controlling intermediate exchange in assembly-line systems.
  • This work guides the reprogramming of enzymatic pathways for biosynthetic chemistry and metabolic engineering.