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Isolation and properties of prephenate dehydratase from Flavobacterium devorans r are described. The enzyme was enriched 43-fold by ammonium sulfate precipitation, by gel chromatography on ultrogel ACA-34 and by hydrophobic chromatography on decylagarose. The molecular weight was estimated to be 1.35 x 10(5). The enzyme was activated in 1mM solutions of L-tyrosine 4,4-fold, of L-phenylalanine 3.9fold and by L-tryptophan 1.9-fold in 0.02M Tris/HCl buffer at pH 7.7. The Km values were, when adding the activator, at L-tyrosine 1.5 x 10(-5) M, at L-phenylalanine 1.3 x 10(-5) M and at L-tryptophan 1 x 10(-5) M. Regulation of aromatic amino acid is discussed in connection with the prephenate dehydratase.
G Krauss, and
R Süssmuth, and
F Lingens
October 2009,
The Plant journal : for cell and molecular biology,
G Krauss, and
R Süssmuth, and
F Lingens
January 1987,
Methods in enzymology,
G Krauss, and
R Süssmuth, and
F Lingens
November 1978,
Archives of biochemistry and biophysics,
G Krauss, and
R Süssmuth, and
F Lingens
December 1974,
Shigaku = Odontology; journal of Nihon Dental College,
G Krauss, and
R Süssmuth, and
F Lingens
January 1991,
Preparative biochemistry,
G Krauss, and
R Süssmuth, and
F Lingens
May 1976,
Journal of bacteriology,
G Krauss, and
R Süssmuth, and
F Lingens
April 1977,
Mikrobiyoloji bulteni,
G Krauss, and
R Süssmuth, and
F Lingens
March 1977,
Rinsho byori. The Japanese journal of clinical pathology,
G Krauss, and
R Süssmuth, and
F Lingens
February 1978,
Anales espanoles de pediatria,
G Krauss, and
R Süssmuth, and
F Lingens
June 1975,
Rinsho byori. The Japanese journal of clinical pathology,
