Disease relevance of Pretyrosine

• Wild-type Brevibacterium flavum has been shown to possess arogenate dehydrogenase activity and to lack prephenate dehydrogenase, thereby providing presumptive evidence that arogenate (previously named "pretyrosine") is an obligatory intermediate of L-tyrosine biosynthesis [1].
• This assay was used to study partially purified arogenate dehydratase from Pseudomonas diminuta, an organism that depends upon the arogenate pathway for L-phenylalanine biosynthesis.(ABSTRACT TRUNCATED AT 250 WORDS)[2]
• Even though both arogenate and prephenate dehydrogenase activities were found in some strains, it seems clear that the arogenate pathway to tyrosine is a common trait that has been highly conserved among cyanobacteria [3].
• The two Arabidopsis thaliana arogenate dehydrogenases TyrAAT1 and TyrAAT2 were overproduced in Escherichia coli and purified to homogeneity [4].
• The method couples the arogenate dehydratase reaction with that of an aromatic aminotransferase partially purified from Acinetobacter calcoaceticus [5].

High impact information on Pretyrosine

• The activity ratios of prephenate dehydratase to arogenate dehydratase remained constant (about 3.3-fold) throughout purification, thus demonstrating a single protein having broad substrate specificity [6].
• Spiro-arogenate is quantitatively converted to phenylalanine at mildly acidic pH and can be converted to arogenate by boiling at basic pH [7].
• The present study reports the first molecular characterization of a plant arogenate dehydrogenase, the enzyme that catalyses the transformation of arogenate into tyrosine [8].
• Molecular and biochemical characterization of an Arabidopsis thaliana arogenate dehydrogenase with two highly similar and active protein domains [8].
• Chorismate mutase, arogenate dehydrogenase, and shikimate dehydrogenase were nearly always unregulated [3].

Biological context of Pretyrosine

• The arogenate dehydratase activity displayed hyperbolic substrate kinetics with a KM for arogenate of 0.32 mM [9].
• The present study reports the first purification and kinetic characterization of two plant arogenate dehydrogenases (EC 1.3.1.43), an enzyme that catalyses the oxidative decarboxylation of arogenate into tyrosine in presence of NADP [4].
• The substrate arogenate was modeled into the active site [10].
• A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis [11].

Associations of Pretyrosine with other chemical compounds

• A novel natural product structurally related to prephenate and arogenate was isolated from a mutant of Neurospora crassa [12].
• Thus, subgroup Ia species lack an unregulated isozyme of chorismate mutase and arogenate dehydratase, enzymes which are thought to divert chorismate to L-phenylalanine under conditions of high carbon input into aromatic biosynthesis [13].

Gene context of Pretyrosine

• The molecular weight of arogenate dehydrogenase is about 68,000, and SDS gel electrophoresis indicates a composition of two identical subunits [14].

Analytical, diagnostic and therapeutic context of Pretyrosine

• Arogenate dehydrogenase from sorghum eluted, with high recovery of activity (93%), as a single peak on DEAE-cellulose chromatography [15].

References