Skip to search formSkip to main contentSkip to account menu

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

Related topics

Related topics

1 relation
Prephenate Dehydrogenase

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
1992
1992
A monofunctional prephenate dehydrogenase created by cleavage of the 5' 109 bp of the tyrA gene from Erwinia herbicola.
A cohesive phylogenetic cluster that is limited to enteric bacteria and a few closely related genera possesses a bifunctional… 
1991
1991
Kinetic studies on chorismate mutase-prephenate dehydrogenase from Escherichia coli: models for the feedback inhibition of prephenate dehydrogenase by L-tyrosine.
Kinetic studies have been undertaken to elucidate the mechanism of the allosteric inhibition by tyrosine of the prephenate… 
1983
1983
Aromatic Amino Acid Biosynthesis in a 4-Chlorobenzoic Acid Degrading Pseudomonas Species; Phenylalanine and Tyrosine Synthesis via Arogenate.
1968
1968
The biosynthesis of tyrosine in Aerobacter aerogenes. Evidence for a suunit structure of the protein converting chorismate into 4-hydroxyphenylpyruvate.
1968
1968
Phenylalanine-Tyrosine Biosynthesis in NEUROSPORA CRASSA.
IOCHEMICAL investigations of the phenylalanine-tyrosine specific portion of the aromatic pathmway reveal a reaction sequence… 
1967
1967
The biosynthesis of tyrosine in Aerobacter aerogenes: partial purification of the T protein.
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)