Investigating substrate specificity in arogenate versus prephenate dehydratases.

Emily J Clayton, Megan Smith-Uffen, Travis W Tribble, Martin L Duennwald, Susanne E Kohalmi

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Article in BMC biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 authors.

Emily J ClaytonDepartment of Biology, University of Western Ontario, 1151 Richmond Street North, London, ON, N6A 5B7, Canada. emily.clayton@concordia.ca.

Megan Smith-UffenDepartment of Biology, University of Western Ontario, 1151 Richmond Street North, London, ON, N6A 5B7, Canada.

Travis W TribbleDepartment of Biology, University of Western Ontario, 1151 Richmond Street North, London, ON, N6A 5B7, Canada.

Martin L DuennwaldDepartment of Biology, University of Western Ontario, 1151 Richmond Street North, London, ON, N6A 5B7, Canada.

Susanne E KohalmiDepartment of Biology, University of Western Ontario, 1151 Richmond Street North, London, ON, N6A 5B7, Canada.

Funding

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6 · The paper itself

Abstract

backgroundPhenylalanine is an essential aromatic amino acid that can only be synthesized de novo by microorganisms and plants. In microorganisms, phenylalanine is synthesized through the prephenate pathway, requiring the activity of a prephenate dehydratase (PDT). In plants, phenylalanine is synthesized instead mostly through the arogenate pathway, requiring the enzyme arogenate dehydratase (ADT). In Arabidopsis, there is a family of six ADTs that catalyze this final step of phenylalanine biosynthesis. However, two of the AtADTs, AtADT1 and AtADT2, can also act as PDTs. All six AtADTs have a high sequence similarity, making it difficult to determine in silico which amino acids determine substrate specificity.

resultsHere, we use domain swapping, targeted mutagenesis, and pha2 yeast complementation to investigate amino acids that confer PDT activity in pha2 yeast. In addition, we established a novel in vivo test of ADT activity to determine how these amino acid changes affect ADT and PDT activity of the AtADTs.

conclusionsOur results demonstrate that a combination of amino acids in the regulatory ACT domain contributes to both ADT and PDT activity in the AtADTs.

Indexed as

ArabidopsisArabidopsis ProteinsHydro-LyasesPhenylalaninePrephenate DehydrataseSaccharomyces cerevisiaeSubstrate SpecificityArabidopsis ProteinsHydro-LyasesPhenylalaninePrephenate DehydrataseACAI assayACT domainArabidopsis thalianaArogenate dehydratasePrephenate dehydrataseSaccharomyces cerevisiaeScreening by complementationSequence-function relationship

Identifiers

PMID42204708

DOI10.1186/s12915-026-02586-8

PMCPMC13217925

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LicenceCC BY-NC-ND

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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.