prephenate dehydrogenase activity

Known as: chorismate mutase--prephenate dehydrogenase activity, prephenate:NAD+ oxidoreductase (decarboxylating) 
Catalysis of the reaction: NAD(+) + prephenate = (4-hydroxyphenyl)pyruvate + CO(2) + NADH. [EC:1.3.1.12, RHEA:13872]
National Institutes of Health

Topic mentions per year

Topic mentions per year

1968-2002
01219682002

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2002
2002
The present study reports the first purification and kinetic characterization of two plant arogenate dehydrogenases (EC 1.3.1.43… (More)
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2002
2002
The present study reports the first molecular characterization of a plant arogenate dehydrogenase, the enzyme that catalyses the… (More)
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1992
1992
A cohesive phylogenetic cluster that is limited to enteric bacteria and a few closely related genera possesses a bifunctional… (More)
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1991
1991
Kinetic studies have been undertaken to elucidate the mechanism of the allosteric inhibition by tyrosine of the prephenate… (More)
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1987
1987
Fragments of the tyrA gene of Escherichia coli, when suitably engineered, can express either the chorismate mutase activity or… (More)
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1984
1984
The prephenate dehydrogenase activity of the bifunctional enzyme chorismate mutase-prephenate dehydrogenase from Escherichia coli… (More)
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1983
1983
The aromatic amino acid biosynthesis was studied in Pseudomonas sp. strain CBS 3 which is able to grow on 4-chlorobenzoic acid… (More)
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1982
1982
We examined the enzymology and regulatory patterns of the aromatic amino acid pathway in 48 strains of cyanobacteria including… (More)
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1980
1980
The regulation of tyrosine production in the anthramycin-producing organism Streptomyces refuineus var. thermotolerans has been… (More)
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1977
1977
Pretyrosine, an intermediate of L-tyrosine biosynthesis in blue-green algae, was found to be enzymatically formed and utilized in… (More)
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