The Tryptophanase-tryptophan Reaction 7. FURTHER EVIDENCE REGARDING THE MECHANISM OF THE ENZYMIC DEGRADATION OF TRYPTOPHAN TO INDOLE: CRITICISM OF THE THEORY THAT ,-o-AMINOPHENYLACETALDEHYDE IS THE INDOLE-FORMING INTERMEDIATE
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Function of Pyridoxal Phosphate: Resolution and Purification of the Tryptophanase Enzyme of Escherichia Coli
Since Hopkins and Cole (1) demonstrated the formation of indole from tryptophan by Bacterium coli, numerous investigators have attempted to find the mechanism of this reaction (2-5). At least three mechanisms have been suggested. Woods (3) postulated an oxidat,ive degradation of tryptophan to yield indole, carbon dioside, water, and ammonia, 5 atoms of oxygen being used in the process. Baker an...
متن کاملReversibility 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...
متن کاملTryptophanase-Catalyzed l-Tryptophan Synthesis from d-Serine in the Presence of Diammonium Hydrogen Phosphate
Tryptophanase, an enzyme with extreme absolute stereospecificity for optically active stereoisomers, catalyzes the synthesis of l-tryptophan from l-serine and indole through a beta-substitution mechanism of the ping-pong type, and has no activity on d-serine. We previously reported that tryptophanase changed its stereospecificity to degrade d-tryptophan in highly concentrated diammonium hydroge...
متن کاملReaction 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...
متن کامل8o. THE COLI-TRYPTOPHAN-INDOLE REACTION 3. ESSENTIAL STRUCTURAL CONDITIONS FOR THE ENZYMIC DEGRADATION OF TRYPTOPHAN TO INDOLE BY JOHN WILLIAM BAKER AND FRANK CHARLES HAPPOLD
THE reaction whereby l-tryptophan is broken down to indole by E. coli has been studied independently by Woods [1935, 1, 2] and by Happold & Hoyle [1935]. Woods worked with washed viable cells of the organism, whereas the latter investigators used suspensions killed in various ways but which, nevertheless, retained the property of catalysing this reaction. By coincidence both investigations, alt...
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