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Related Concept Videos

Regioselective Formation of Enolates01:33

Regioselective Formation of Enolates

As depicted in the figure below, the unsymmetrical ketones can form two possible enolates: less substituted or more substituted enolates. Usually, the thermodynamic enolates are formed from the more substituted α-carbon atom, while the kinetic enolates are formed faster by deprotonation from the less substituted position. The thermodynamic enolates have lower energy, so they are more stable. But the energy required to form kinetic enolates is less.
Alkynes to Aldehydes and Ketones: Acid-Catalyzed Hydration02:40

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Regioselectivity and Stereochemistry of Acid-Catalyzed Hydration02:34

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Allosteric Proteins-ATCase01:19

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Reduction of Alkenes: Asymmetric Catalytic Hydrogenation02:17

Reduction of Alkenes: Asymmetric Catalytic Hydrogenation

Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
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Related Experiment Video

Updated: May 29, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
05:51

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Published on: December 19, 2011

Investigating substrate specificity in arogenate versus prephenate dehydratases.

Emily J Clayton1,2, Megan Smith-Uffen3, Travis W Tribble3

  • 1Department of Biology, University of Western Ontario, 1151 Richmond Street North, London, ON, N6A 5B7, Canada. emily.clayton@concordia.ca.

BMC Biology
|May 28, 2026
PubMed
Summary
This summary is machine-generated.

Amino acid combinations in the regulatory ACT domain of Arabidopsis thaliana arogenate dehydratases (AtADTs) determine both arogenate dehydratase (ADT) and prephenate dehydratase (PDT) activity. This finding clarifies substrate specificity in phenylalanine biosynthesis.

Keywords:
Arabidopsis thalianaSaccharomyces cerevisiaeACAI assayACT domainArogenate dehydratasePrephenate dehydrataseScreening by complementationSequence-function relationship

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Area of Science:

  • Biochemistry
  • Plant Molecular Biology

Background:

  • Phenylalanine biosynthesis occurs via distinct pathways in microorganisms (prephenate pathway) and plants (arogenate pathway).
  • Arabidopsis thaliana possesses six arogenate dehydratase (ADT) enzymes, with some exhibiting dual ADT and prephenate dehydratase (PDT) activity.
  • High sequence similarity among AtADTs complicates in silico prediction of substrate specificity.

Purpose of the Study:

  • To identify specific amino acids conferring prephenate dehydratase (PDT) activity in Arabidopsis thaliana arogenate dehydratases (AtADTs).
  • To elucidate the role of these amino acids in determining both arogenate dehydratase (ADT) and PDT activity.

Main Methods:

  • Domain swapping and targeted mutagenesis were employed to alter AtADT sequences.
  • Yeast complementation assays (pha2 yeast) were used to assess PDT activity.
  • A novel in vivo assay was developed to evaluate ADT activity.

Main Results:

  • Specific amino acid residues within the regulatory ACT domain were identified as critical for enzyme function.
  • These amino acid changes influenced both ADT and PDT activities of the AtADTs.
  • The study successfully linked specific amino acid combinations to substrate specificity.

Conclusions:

  • A combination of amino acids within the regulatory ACT domain is essential for both ADT and PDT activity in AtADTs.
  • This highlights the structural basis for substrate specificity in phenylalanine biosynthesis enzymes.