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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 Oct;83(19):7231–7235. doi: 10.1073/pnas.83.19.7231

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

E Jung, L O Zamir, R A Jensen
PMCID: PMC386689  PMID: 3463961

Abstract

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 Nicotiana silvestris. Prephenate dehydratase (which converts prephenate to phenylpyruvate) was not detected. Arogenate dehydratase was also found in washed spinach chloroplasts, and these data add to emerging evidence in support of the existence in the plastidial compartment of a complete assembly of enzymes comprising aromatic amino acid biosynthesis. Arogenate dehydratase from tobacco and spinach were both specific for L-arogenate, inhibited by L-phenylalanine, and activated by L-tyrosine. Apparent Km values for L-arogenate (0.3 X 10(-3) M), pH optima (pH 8.5-9.5), and temperature optima for catalysis (32-34 degrees C) were also similar.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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