The prephenate dehydrogenase component of the bifunctional T‐protein in enteric bacteria can utilize L‐arogenate

[1]  R. Jensen,et al.  The evolutionary history of two bifunctional proteins that emerged in the purple bacteria , 1986 .

[2]  R. Jensen,et al.  Biochemical pathways in prokaryotes can be traced backward through evolutionary time. , 1985, Molecular biology and evolution.

[3]  B. E. Davidson,et al.  Chorismate mutase/prephenate dehydrogenase from Escherichia coli K12: purification, characterization, and identification of a reactive cysteine. , 1984, Biochemistry.

[4]  A. W. Douglas,et al.  Structure of arogenate (pretyrosine), an amino acid intermediate of aromatic biosynthesis , 1980 .

[5]  D. Pierson,et al.  Dual enzymatic routes to L-tyrosine and L-phenylalanine via pretyrosine in Pseudomonas aeruginosa. , 1977, The Journal of biological chemistry.

[6]  M. M. Bradford.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[7]  B. E. Davidson,et al.  Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. I. Purification, molecular weight, and amino acid composition. , 1972, The Journal of biological chemistry.

[8]  F. Gibson,et al.  Tyrosine biosynthesis in Aerobacter aerogenes. Purification and properties of chorismate mutase-prephenate dehydrogenase. , 1970, Biochimica et biophysica acta.

[9]  R. Cotton,et al.  THE BIOSYNTHESIS OF PHENYLALANINE AND TYROSINE; ENZYMES CONVERTING CHORISMIC ACID INTO PREPHENIC ACID AND THEIR RELATIONSHIPS TO PREPHENATE DEHYDRATASE AND PREPHENATE DEHYDROGENASE. , 1965, Biochimica et biophysica acta.

[10]  R. Jensen,et al.  The postprephenate biochemical pathways to phenylalanine and tyrosine: an overview. , 1987, Methods in enzymology.

[11]  D. B. Sprinson,et al.  [70a] Preparation of prephenic acid , 1970 .