4.2.1.51: prephenate dehydratase
This is an abbreviated version!
For detailed information about prephenate dehydratase, go to the full flat file.
Word Map on EC 4.2.1.51
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4.2.1.51
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l-phenylalanine
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arogenate
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l-tyrosine
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dahp
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l-phe
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7-phosphate
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cyclohexadienyl
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l-tyr
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3-deoxy-d-arabino-heptulosonate
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feedback-inhibited
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5.4.99.5
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synthesis
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industry
- 4.2.1.51
- l-phenylalanine
- arogenate
- l-tyrosine
- dahp
- l-phe
- 7-phosphate
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cyclohexadienyl
- l-tyr
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3-deoxy-d-arabino-heptulosonate
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feedback-inhibited
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5.4.99.5
- synthesis
- industry
Reaction
Synonyms
ADT1, ADT2, ADT6, AroQ, chorismate mutase prephenate dehydratase, chorismate mutase-prephenate dehydratase, Chorismate mutase/prephenate dehydratase, CM-PD, CM/PDT/PDHG, Cmut1, CM–PDT, Ct-PDT, cyclohexydienyl dehydratase, dehydratase, prephenate, Gmut11, Gmut9, MjPDT, monofunctional prephenate dehydratase, MtbPDT, P-protein, P-protein dehydratase, PDT, PDT protein, PheA, PpADT-B, PpADT-C, PpADT-G, prephenate dehydratase, prephenate dehydratase 1, Sa-PDT
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General Information
General Information on EC 4.2.1.51 - prephenate dehydratase
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evolution
all plant clades include PAC domain-containing arogenate dehydratases, suggesting that the prephenate dehydratase activity, and thus the ability to synthesize L-phenylalanine using phenylpyruvate as an intermediate, has been preserved throughout the evolution of plants. This pathway together with the arogenate pathway gives plants a broad and versatile capacity to synthesize L-phenylalanine and its derived compounds
malfunction
metabolism
physiological function
additional information
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a decrease in catechins content, 2-phenylethanol, and PDT activity is observed in the tea shoots infested by Exobasidium vexans over healthy shoots. Drought stress induced by withholding water for a period of 8 days causes initial increase in the contents of the catechins and 2-phenylethanol, and in PDT activity, but decreases with 3 day onwards with an increase in the severity of water stress, detailed overview
use of a T326P mutation in the regulation domain of pheA (pheAfbr) for L-phenylalanine production. Overexpression of pheAfbr and/or wild-type aroF is helpful for the enhancement of the key enzymes in L-phenylalanine biosynthesis
malfunction
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use of a T326P mutation in the regulation domain of pheA (pheAfbr) for L-phenylalanine production. Overexpression of pheAfbr and/or wild-type aroF is helpful for the enhancement of the key enzymes in L-phenylalanine biosynthesis
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transgenic Arabidopsis plants expressing a truncated, feedback-insensitive chorismate mutase/prephenate dehydratase gene accumulate Phe (up to 100fold compared to control plants) and are more sensitive than wild-type plants to the Trp biosynthesis inhibitor 5-methyl-Trp. Thus Phe biosynthesis competes with Trp biosynthesis from their common precursor chorismate. A number of secondary metabolites derived from all three aromatic amino acids (Phe, Trp and Tyr) are altered in the transgenic plants, implying regulatory cross-interactions between the flux of aromatic amino acid biosynthesis from chorismate and their further metabolism into various secondary metabolites. Truncated PheA expression has a minimal effect on primary metabolism and on the Arabidopsis transcriptome. A high proportion of the feedback-insensitive chorismate mutase/prephenate dehydratase polypeptide produced by this transgene is translocated into the plastids
metabolism
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prephenate dehydratase takes part in the biosynthetic pathway of flavan-3-ols, overview
metabolism
the enzyme is involved in aromatic amino acid biosynthesis
metabolism
the enzyme is involved in L-phenylalanine biosynthesis pathway
metabolism
the enzyme is involved in the phenylpyruvate biosynthetic pathway
Vitis vinifera x Vitis vinifera
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involved in aromatic amino acid metabolism
physiological function
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involved in aromatic amino acid metabolism