FAQ

prephenate dehydratase activity

Known as: prephenate hydro-lyase (decarboxylating), prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming) 
Catalysis of the reaction: prephenate = phenylpyruvate + H2O + CO2. [EC:4.2.1.51]
National Institutes of Health

Topic mentions per year

Topic mentions per year

1968-2016
012319682016

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1 relation
Prephenate Dehydratase

Related mentions per year

Related mentions per year

1965-2018
1960198020002020
prephenate dehydratase activity
Prephenate Dehydratase

Papers overview

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2016
2016
Identification of a small protein domain present in all plant lineages that confers high prephenate dehydratase activity.
l-Phenylalanine serves as a building block for the biosynthesis of proteins, but also as a precursor for a wide range of plant… (More)
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2004
2004
Biosynthesis of aromatic amino acids in Nocardia sp. 239: effects of amino acid analogues on growth and regulatory enzymes
Further steps required for overproduction of aromatic amino acids by a mutant strain of Nocardia sp. 239 (Noc 87-13), unable to… (More)
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2003
2003
Chorismate Mutase-Prephenate Dehydratase
  • STAN W. ARTZ
  • 2003
Chorismate mutase-prephenate dehydratase catalyzes the first two reactions specific for phenylalanine synthesis in Salmonella… (More)
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1996
1996
Cloning of m-fluorophenylalanine-resistant gene and mutational analysis of feedback-resistant prephenate dehydratase from Corynebacterium glutamicum.
Corynebacterium glutamicum was mutated by nitrosoguanidine and five m-fluorophenylalanine (mFP)-resistant mutants were isolated… (More)
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1995
1995
Location of the active site of allosteric chorismate mutase from Saccharomyces cerevisiae, and comments on the catalytic and regulatory mechanisms.
The active site of the allosteric chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5) from yeast Saccharomyces cerevisiae… (More)
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1992
1992
Novel mutations in the pheA gene of Escherichia coli K-12 which result in highly feedback inhibition-resistant variants of chorismate mutase/prephenate dehydratase.
The bifunctional enzyme chorismate mutase/prephenate dehydratase (EC 5.4.99.5/4.2.1.51), which is encoded by the pheA gene of… (More)
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1991
1991
A single cyclohexadienyl dehydratase specifies the prephenate dehydratase and arogenate dehydratase components of one of two independent pathways to L-phenylalanine in Erwinia herbicola.
Dual biosynthetic pathways diverge from prephenate to L-phenylalanine in Erwinia herbicola, the unique intermediates of these… (More)
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1983
1983
Evolution of L-phenylalanine biosynthesis in rRNA homology group I of Pseudomonas
Group I pseudomonads exhibit diversity for L-phenylalanine biosynthesis that is a basis for separation of two subgroups. Subgroup… (More)
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1979
1979
Enzyme-enzyme interaction and the biosynthesis of aromatic amino acids in Escherichia coli.
The technique of affinity chromatography has been used to demonstrate that enzymes involved in the biosynthesis of tyrosine and… (More)
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1973
1973
Channel-shuttle mechanism for the regulation of phenylalanine and tyrosine synthesis at a metabolic branch point in Pseudomonas aeruginosa.
A bifunctional protein complex was partially purified from Pseudomonas aeruginosa. Catalytic activities for chorismate mutase and… (More)
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