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Literature summary for 4.2.1.51 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
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Cloned(Commentary)

Cloned (Comment) Organism
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

Inhibitors Comment Organism Structure
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)

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

Organism

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

Reaction Comment Organism Reaction ID
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
a

Substrates and Products (Substrate)

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