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Chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5) was extracted from Chlamydomonas reinhardi by sonication. Fractionation of crude sonic extracts with (NH4)2SO4 and by DEAE-cellulose and Sephadex gel chromatography indicated a single peak of chorismate mutase activity with molecular weight 61 000. The Michaelis constant for 20-fold purified enzyme was 0.46 mM. Prephenate dehydrogenase (EC 1.3.1.9) and prephenate dehydratase (EC 4.2.1.40) activities were not detected in our crude or partially purified preparations of chorismate mutase. Tyrosine (1.25 mM) inhibited chorismate mutase activity by approx. 85% in crude and partially purified preparations. Phenylalanine (1.25 mM) inhibited 20%. Tryptophan (1.25 mM) by itself had no detectable effect on chorismate mutase activity but it completely reversed inhibition by tyrosine and phenylalanine. No repression of chorismate mutase was observed when the minimal growth medium was supplemented with aromatic end products.
G Zurawski, and
K D Brown
January 1969,
Biochemistry,
G Zurawski, and
K D Brown
December 1985,
Archives of biochemistry and biophysics,
G Zurawski, and
K D Brown
October 1970,
European journal of biochemistry,
G Zurawski, and
K D Brown
July 1980,
Journal of biochemistry,
G Zurawski, and
K D Brown
June 1984,
Biochimica et biophysica acta,
G Zurawski, and
K D Brown
April 1970,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
G Zurawski, and
K D Brown
September 1970,
Biochimica et biophysica acta,
G Zurawski, and
K D Brown
January 1972,
Archiv fur Mikrobiologie,
G Zurawski, and
K D Brown
May 1976,
Journal of bacteriology,
G Zurawski, and
K D Brown
December 1966,
Plant physiology,
