Literature summary for 5.4.99.5 extracted from

Tzin, V.; Malitsky, S.; Aharoni, A.; Galili, G.
Expression of a bacterial bi-functional chorismate mutase/prephenate dehydratase modulates primary and secondary metabolism associated with aromatic amino acids in Arabidopsis (2009), Plant J., 60, 156-167.

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Arabidopsis thaliana	Escherichia coli
generation of transgenic Arabidopsis plants expressing a bacterial feedback-insensitive chorismate mutase/prephenate dehydratase gene (truncated PheA) under the control of the 35S CaMV promoter, fused inframe at the 3' end of the coding sequence to DNA encoding a hemagglutinin epitope tag. Two chimeric constructs: in one, DNA encoding a Rubisco small subunit-3A plastid transit peptide is fused in-frame to the 5' end of the PheA open reading frame to direct the bacterial enzyme in to the plastid where aromatic amino acid biosynthesis is localized. The second construct lacks the Rubisco small subunit-3A plastid transit peptide in order to test whether aromatic amino acid metabolism is strictly localized to the plastid or whether at least some parts of it operate in the cytosol. Both constructs transformed into Arabidopsis plants, and homozygous T2 plants are generated	Escherichia coli

Cloned (Comment)

Organism

expressed in Arabidopsis thaliana

Escherichia coli

generation of transgenic Arabidopsis plants expressing a bacterial feedback-insensitive chorismate mutase/prephenate dehydratase gene (truncated PheA) under the control of the 35S CaMV promoter, fused inframe at the 3' end of the coding sequence to DNA encoding a hemagglutinin epitope tag. Two chimeric constructs: in one, DNA encoding a Rubisco small subunit-3A plastid transit peptide is fused in-frame to the 5' end of the PheA open reading frame to direct the bacterial enzyme in to the plastid where aromatic amino acid biosynthesis is localized. The second construct lacks the Rubisco small subunit-3A plastid transit peptide in order to test whether aromatic amino acid metabolism is strictly localized to the plastid or whether at least some parts of it operate in the cytosol. Both constructs transformed into Arabidopsis plants, and homozygous T2 plants are generated

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Chorismate	-	Escherichia coli	Prephenate	-	?

Synonyms

Synonyms	Comment	Organism
Chorismate mutase/prephenate dehydratase	-	Escherichia coli
CM/PDT	bi-functional chorismate mutase/prephenate dehydratase	Escherichia coli
PheA	-	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	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	Escherichia coli