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Related Experiment Video

Updated: Feb 13, 2026

Standardized Modular Assembly of Polycistronic Operons with Modular Cloning (MoClo) using the In-Cloning toolkit
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Exploring modular allostery via interchangeable regulatory domains.

Yifei Fan1,2, Penelope J Cross1,2, Geoffrey B Jameson3

  • 1Biomolecular Interaction Centre, University of Canterbury, 8140 Christchurch, New Zealand.

Proceedings of the National Academy of Sciences of the United States of America
|March 7, 2018
PubMed
Summary
This summary is machine-generated.

Protein domains can be swapped to engineer new allosteric regulation in enzymes. This study demonstrates domain interchangeability in 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS), creating novel enzyme functions.

Keywords:
allosterybifunctional enzymeprotein engineeringshikimatesynthetic biology

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Proteins are composed of domains, which can combine to form new functions.
  • Allosteric regulation is crucial for controlling enzyme activity.
  • 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS) is a key enzyme in aromatic amino acid biosynthesis with diverse allosteric mechanisms.

Purpose of the Study:

  • To investigate the functional interchangeability of regulatory domains in DAH7PS.
  • To engineer novel allosteric mechanisms and ligand specificities by swapping regulatory domains.
  • To explore domain swapping as a strategy for creating bifunctional enzymes.

Main Methods:

  • Creation of protein chimeras by interchanging regulatory domains of DAH7PS.
  • Assessment of catalytic activity of engineered DAH7PS variants.
  • Characterization of allosteric regulation and ligand specificity in the chimera proteins.

Main Results:

  • Engineered DAH7PS chimeras retained catalytic activity.
  • The swapped regulatory domains conferred new, functional allostery.
  • Ligand specificity and allosteric mechanisms were successfully switched based on the incorporated regulatory domain.

Conclusions:

  • Protein domain interchangeability is an effective strategy for engineering allostery in multidomain proteins.
  • This approach can create novel enzyme functions and bifunctional enzymes.
  • Understanding domain modularity facilitates protein engineering and the evolution of new biological functions.