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Information on EC 4.2.1.51 - prephenate dehydratase and Organism(s) Buchnera aphidicola and UniProt Accession P57472

for references in articles please use BRENDA:EC4.2.1.51
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.51 prephenate dehydratase
IUBMB Comments
This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate.
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This record set is specific for:
Buchnera aphidicola
UNIPROT: P57472
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Word Map
The taxonomic range for the selected organisms is: Buchnera aphidicola
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
prephenate dehydratase, chorismate mutase-prephenate dehydratase, chorismate mutase prephenate dehydratase, cm-pd, mtbpdt, pdt protein, mjpdt, monofunctional prephenate dehydratase, sa-pdt, ct-pdt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CM-PD
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-
-
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cyclohexydienyl dehydratase
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-
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dehydratase, prephenate
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-
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monofunctional prephenate dehydratase
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P-protein
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-
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PDT
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
prephenate = phenylpyruvate + H2O + CO2
show the reaction diagram
this enzyme in the enteric bacteria also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
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SYSTEMATIC NAME
IUBMB Comments
prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming)
This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate.
CAS REGISTRY NUMBER
COMMENTARY hide
9044-88-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
prephenate
phenylpyruvate + H2O + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
prephenate
phenylpyruvate + H2O + CO2
show the reaction diagram
involved in vivo production of high levels of phenylalanine
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
endosymbiont isolated from aphid Acyrthosiphon pisum
SwissProt
Manually annotated by BRENDA team
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Bacteriol.
182
2967-2969
2000
Buchnera aphidicola (P57472), Buchnera aphidicola
Manually annotated by BRENDA team