ArticleProceedings of the National Academy of Sciences of the United States of America2013
Engineering allosteric control to an unregulated enzyme by transfer of a regulatory domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 52 citations in OpenAlex.
- The more we learn, the more diverse it gets: structures, functions and evolution in the Phosphofructokinase Superfamily.The Biochemical journal · 2025Review
- Insight into the role of the Bateman domain at the molecular and physiological levels through engineered IMP dehydrogenases.Protein science : a publication of the Protein Society · 2023Article
- In-Depth Computational Analysis of Natural and Artificial Carbon Fixation Pathways.Biodesign research · 2021Article
- Domain cross-talk within a bifunctional enzyme provides catalytic and allosteric functionality in the biosynthesis of aromatic amino acids.The Journal of biological chemistry · 2019Article
- Engineering Allostery into Proteins.Advances in experimental medicine and biology · 2019Review
- Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018Review
- Exploring modular allostery via interchangeable regulatory domains.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit.eLife · 2018Article
- A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.Frontiers in molecular biosciences · 2018Review
- X-ray Scattering Studies of Protein Structural Dynamics.Chemical reviews · 2017Review
- Core Genes Evolve Rapidly in the Long-Term Evolution Experiment with Escherichia coli.Genome biology and evolution · 2017Article
- Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.Scientific reports · 2016Article
- Article
- The Functional Unit of Neisseria meningitidis 3-Deoxy-ᴅ-Arabino-Heptulosonate 7-Phosphate Synthase Is Dimeric.PloS one · 2016Article
- Stochastic focusing coupled with negative feedback enables robust regulation in biochemical reaction networks.Journal of the Royal Society, Interface · 2015Article
- Crystal structure ofBiotechnology reports (Amsterdam, Netherlands) · 2014Article
- Protein engineering: a new frontier for biological therapeutics.Current drug metabolism · 2014Review
- Neisseria meningitidis expresses a single 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase that is inhibited primarily by phenylalanine.Protein science : a publication of the Protein Society · 2013Article
- The diversity of allosteric controls at the gateway to aromatic amino acid biosynthesis.Protein science : a publication of the Protein Society · 2013Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Allosteric regulation of protein function is a critical component of metabolic control. Its importance is underpinned by the diversity of mechanisms and its presence in all three domains of life. The first enzyme of the aromatic amino acid biosynthesis, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase, shows remarkable variation in allosteric response and machinery, and both contemporary regulated and unregulated orthologs have been described. To examine the molecular events by which allostery can evolve, we have generated a chimeric protein by joining the catalytic domain of an unregulated 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with the regulatory domain of a regulated enzyme. We demonstrate that this simple gene fusion event on its own is sufficient to confer functional allostery to the unregulated enzyme. The fusion protein shares structural similarities with its regulated parent protein and undergoes an analogous major conformational change in response to the binding of allosteric effector tyrosine to the regulatory domain. These findings help delineate a remarkably facile mechanism for the evolution of modular allostery by domain recruitment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.