The tryptophanase-tryptophan reaction. 9. The nature, characteristics and partial purification of the tryptophanase complex.

نویسندگان

  • E A Dawes
  • F C Happold
چکیده

The name tryptophanase was given by Happold & Hoyle (1935) to the enzyme complex of Escherichia coli which induces and catalyzes the production of indole from tryptophan by non-viable bacterial preparations with the consumption of five atoms of oxygen (Woods, 1935). The present communication describes the preparation of this complex in the cell-free state, and subsequent investigation of the components present by a study of the action of various recognized inhibitors, followed by resolution and identification of the coenzyme factors involved. A preliminary announcement of some of the results has been made (Dawes, Dawson & Happold, 1947a). The investigation of the nature of the tryptophanase complex (Dawes, Dawson & Happold, 1947b, c) was followed by an examination of its characteristics, and attempts at purification were carried out by ammonium sulphate fractionation. Wood, Gunsalus & Umbreit (1947) have already published results of a partial purification of the enzyme effecting fission of the tryptophan molecule using a similar technique to ours; we and they have shown independently that pyridoxal phosphate is the coenzyme for the reaction, while they have shown also that the products of the reaction are one mole each of indole, pyruvic acid and ammonia.

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Reaction pathway of tryptophanase-catalyzed L-tryptophan synthesis from D-serine.

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Function of Pyridoxal Phosphate: Resolution and Purification of the Tryptophanase Enzyme of Escherichia Coli

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Properties of Crystalline Tryptophanase.

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عنوان ژورنال:
  • The Biochemical journal

دوره 44 3  شماره 

صفحات  -

تاریخ انتشار 1949