Prephenate aminotransferase directs plant phenylalanine biosynthesis via arogenate.
نویسندگان
چکیده
The aromatic amino acids L-phenylalanine and L-tyrosine and their plant-derived natural products are essential in human and plant metabolism and physiology. Here we identified Petunia hybrida and Arabidopsis thaliana genes encoding prephenate aminotransferases (PPA-ATs), thus completing the identification of the genes involved in phenylalanine and tyrosine biosyntheses. Biochemical and genetic characterization of enzymes showed that PPA-AT directs carbon flux from prephenate toward arogenate, making the arogenate pathway predominant in plant phenylalanine biosynthesis.
منابع مشابه
Tyrosine biosynthesis in Sorghum bicolor: isolation and regulatory properties of arogenate dehydrogenase.
The conversion of prephenic acid to tyrosine can occur by two different routes: (a) oxidative decarboxylation (prephenate dehydrogenase) followed by transamination (aromatic aminotransferase); (b) transamination of prephenate forming the non-aromatic amino acid arogenic acid (prephenate aminotransferase) followed by oxidative decarboxylation (arogenate dehydrogenase). High activity of arogenate...
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The specific enzymological route of L-phenylalanine biosynthesis has not been established in any higher plant system. The possible pathway routes that have been identified in microorganisms utilize either phenylpyruvate or L-arogenate as a unique intermediate. We now report the presence of arogenate dehydratase (which converts L-arogenate to L-phenylalanine) in cultured-cell populations of Nico...
متن کاملPhylobiochemical characterization of class-Ib aspartate/prephenate aminotransferases reveals evolution of the plant arogenate phenylalanine pathway.
The aromatic amino acid Phe is required for protein synthesis and serves as the precursor of abundant phenylpropanoid plant natural products. While Phe is synthesized from prephenate exclusively via a phenylpyruvate intermediate in model microbes, the alternative pathway via arogenate is predominant in plant Phe biosynthesis. However, the molecular and biochemical evolution of the plant arogena...
متن کاملTyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase.
A stable activity which transfers the amino group from glutamate to prephenate was extracted from 4-day old etiolated shoots of sorghum. The activity was retained on DEAE cellulose and eluted as a single peak. Prephenate aminotransferase co-eluted with a very abundant alpha-ketoglutarate: aspartate aminotransferase, but heating at 70 degrees C resulted in loss of alpha-ketoglutarate: aspartate ...
متن کاملRNAi suppression of Arogenate Dehydratase1 reveals that phenylalanine is synthesized predominantly via the arogenate pathway in petunia petals.
l-Phe, a protein building block and precursor of numerous phenolic compounds, is synthesized from prephenate via an arogenate and/or phenylpyruvate route in which arogenate dehydratase (ADT) or prephenate dehydratase, respectively, plays a key role. Here, we used Petunia hybrida flowers, which are rich in Phe-derived volatiles, to determine the biosynthetic routes involved in Phe formation in p...
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ورودعنوان ژورنال:
- Nature chemical biology
دوره 7 1 شماره
صفحات -
تاریخ انتشار 2011