Chloroplasts of higher plants synthesize L-phenylalanine via L-arogenate.

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Chloroplasts of higher plants synthesize L-phenylalanine via L-arogenate.

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...

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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 ...

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Co-accumulation of prephenate, L-arogenate, and spiro-arogenate in a mutant of Neurospora.

A mutant strain of Neurospora crassa blocked in each of the initial steps of tryptophan, tyrosine, and phenylalanine biosynthesis was previously shown to accumulate and secrete prephenate and L-arogenate (Jensen, R.A., Zamir, L.O., St. Pierre, M., Patel, N., and Pierson, D.L. (1977) J. Bacteriol. 132, 896-903). We now report the co-accumulation of yet another compound which was identified (Zami...

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Dual enzymatic routes to L-tyrosine and L-phenylalanine via pretyrosine in Pseudomonas aeruginosa.

Pretyrosine, an intermediate of L-tyrosine biosynthesis in blue-green algae, was found to be enzymatically formed and utilized in Pseudomonas aeruginosa. The enzymology and regulation of aromatic biosynthesis were re-evaluated in the context of these new findings, Four species of aromatic aminotranaferase were separated and partially purified. Each was reactive with prephenate, phenylpyruvate, ...

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In the past year, the last missing enzyme of the L-galactose pathway, the linear form of which appears to represent the major biosynthetic route to L-ascorbate (vitamin C) in higher plants, has been identified as a GDP-L-galactose phosphorylase. This enzyme catalyzes the first committed step in the synthesis of that vital antioxidant and enzyme cofactor. Here, we discuss how GDP-L-galactose pho...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1986

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.83.19.7231