نتایج جستجو برای: tryptophanase

تعداد نتایج: 360  

Journal: :avicenna journal of medical biotechnology 0

background: l-tryptophan is used widespread in the pharmaceutical industry. the majority of l-trp production depends on microbial processes that produce l-tryptophan from indole and l-serine. these processes are very costly due to the costs of precursors, especially l-serine. use of inexpensive substitutions as the l-serine source of l-tryptophan production enables us to reach a cost-effective ...

Journal: :The Journal of biological chemistry 1992
A V Kamath C Yanofsky

The tryptophanase (tna) operon of Proteus vulgaris was cloned and characterized and found to be organized similarly to the tna operon of Escherichia coli. Both operons contain two major structural genes, tnaA and tnaB, that encode tryptophanase and a tryptophan permease, respectively. tnaA of P. vulgaris is preceded by a transcribed leader region, encoding a 34-residue leader peptide, TnaC, tha...

Journal: :Environmental microbiology 2015
Ying Hu Brian W Kwan Devon O Osbourne Michael J Benedik Thomas K Wood

Persister cells survive antibiotic and other environmental stresses by slowing metabolism. Since toxins of toxin/antitoxin (TA) systems have been postulated to be responsible for persister cell formation, we investigated the influence of toxin YafQ of the YafQ/DinJ Escherichia coli TA system on persister cell formation. Under stress, YafQ alters metabolism by cleaving transcripts with in-frame ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1972
T Watanabe E E Snell

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...

2012
Akihiko Shimada Haruka Ozaki

The invariance principle of enzyme enantioselectivity must be absolute because it is absolutely essential to the homochiral biological world. Most enzymes are strictly enantioselective, and tryptophanase is one of the enzymes with extreme absolute enantioselectivity for L-tryptophan. Contrary to conventional knowledge about the principle, tryptophanase becomes flexible to catalyze D-tryptophan ...

Journal: :The Journal of biological chemistry 1977
M N Kazarinoff E E Snell

Tryptophanase from Escherichia coli B/1t7-A is inactivated by the arginine-specific reagent, phenylglyoxal, in potassium phosphate buffer at pH 7.8 AND 25 degrees. Apo- and holoenzyme are inactivated at the same rate, and inactivation of both is correlated with modification of 2 arginine residues/tryptophanase monomer. Substrate analogs having a carboxyl group protect the holoenzyme against bot...

Journal: :Chemical communications 2003
Kenneth Kam-Wing Lo Keith Hing-Kit Tsang Wai-Ki Hui Nianyong Zhu

Two novel luminescent rhenium(I) diimine indole complexes have been designed and their properties studied; these conjugates can be recognised by indole-binding proteins including bovine serum albumin, lysozyme and tryptophanase.

Journal: :Journal of Biological Chemistry 1967

Journal: :Journal of Biological Chemistry 1977

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