The ′tryptophanase-tryptophan reaction

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35 . The Tryptophanase - tryptophan Reaction

The facts described by Happold &'Hoyle [1936] and Evans et al. [1941] can be concisely stated as follows: (1) In a complex medium (e.g. bouillon, casein-digest, etc.) in which the presence of glucose in sufficient amount inhibits completely the production of indole by B. coli, the complete tryptophanase system is absent from the cells. (2) With a simple salt medium as used by Fildes, glucose on...

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

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 co...

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Reversibility of the tryptophanase reaction: synthesis of tryptophan from indole, pyruvate, and ammonia.

Degradation of tryptophan to indole, pyruvate, and ammonia by tryptophanase (EC 4....) from Escherichia coli, previously thought to be an irreversible reaction, is readily reversible at high concentrations of pyruvate and ammonia. Tryptophan and certain of its analogues, e.g., 5-hydroxytryptophan, can be synthesized by this reaction from pyruvate, ammonia, and indole or an appropriate derivativ...

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

Tryptophanase, L-tryptophan indole-lyase with extremely absolute stereospecificity, can change the stereospecificity in concentrated diammonium hydrogenphosphate solution. While tryptophanase is not inert to D-serine in the absence of diammonium hydrogenphosphate, it can undergo L-tryptophan synthesis from D-serine along with indole in the presence of it. It has been well known that tryptophana...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1942

ISSN: 0306-3283

DOI: 10.1042/bj0360311