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Literature summary extracted from

  • Jimenez, N.; Gonzalez-Candelas, F.; Silva, F.J.
    Prephenate dehydratase from the aphid endosymbiont (Buchnera) displays changes in the regulatory domain that suggest its desensitization to inhibition by phenylalanine (2000), J. Bacteriol., 182, 2967-2969.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.51 DNA sequence determination and analysis of the two-domain aroQ/pheA gene, constitutive expression due to the absence of an attenuator region, changes in the ESRP sequence leading to desensitization to inhibition by phenylalanine Buchnera aphidicola

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.51 additional information changes in the ESRP sequence, involved in allosteric binding of phenylalanine, lead to desensitization to inhibition by phenylalanine, permitting the overproduction of the amino aid in vivo Buchnera aphidicola

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.51 prephenate Buchnera aphidicola involved in vivo production of high levels of phenylalanine phenylpyruvate + H2O + CO2
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?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.51 Buchnera aphidicola P57472 endosymbiont isolated from aphid Acyrthosiphon pisum
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Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.51 prephenate = phenylpyruvate + H2O + CO2 this enzyme in the enteric bacteria also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate Buchnera aphidicola

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.51 prephenate
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Buchnera aphidicola phenylpyruvate + H2O + CO2
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?
4.2.1.51 prephenate involved in vivo production of high levels of phenylalanine Buchnera aphidicola phenylpyruvate + H2O + CO2
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?