نتایج جستجو برای: tryptophanase

تعداد نتایج: 360  

2016
Frank Elbers Claudia Woite Valentina Antoni Sara Stein Hiroshi Funakoshi Toshikazu Nakamura Gereon Schares Walter Däubener Silvia K Eller

Tryptophan is an essential amino acid for hosts and pathogens. The liver enzyme tryptophan 2,3-dioxygenase (TDO) provokes, by its ability to degrade tryptophan to N-formylkynurenine, the precursor of the immune-relevant kynurenines, direct and indirect antimicrobial and immunoregulatory states. Up to now these TDO-mediated broad-spectrum effector functions have never been observed under hypoxia...

Journal: :Applied and environmental microbiology 2012
Ryan C Fink Elaine P Black Zhe Hou Masayuki Sugawara Michael J Sadowsky Francisco Diez-Gonzalez

An increasing number of outbreaks of gastroenteritis recently caused by Escherichia coli O157:H7 have been linked to the consumption of leafy green vegetables. Although it is known that E. coli survives and grows in the phyllosphere of lettuce plants, the molecular mechanisms by which this bacterium associates with plants are largely unknown. The goal of this study was to identify E. coli genes...

2017
Yi Chen Haixia Xu Mingyue Zhu Kun Liu Bo Lin Ruxian Luo Chuanbai Chen Mengsen Li

Serotonin (5-hydroxytryptamine, 5-HT) dysfunction is associated with the pathophysiology of depression. Tryptophan hydroxylase (TPH), the rate-limiting enzyme in 5-HT biosynthesis, is believed to have essential role in many mental disorders, including depression. In the present study, we generated a rat model of depression by exposing the animals to stress, and the rats were then treated with p...

Journal: :The Journal of biological chemistry 1980
T Nakamura H Shinno A Ichihara

The basal activity of tryptophan 2,3-dioxygenase (EC-1.13.11.11) in primary cultured rat hepatocytes decreased during culture, but addition of either tryptophan (2.5 x 10(-3) M) or dexamethasone (1 x 10(-6) M) could prevent the decrease. Addition of both compounds caused severalfold induction of activity. Glucagon (1 x 10(-8) M) alone did not induce the activity, but its inductive effect in com...

2014
Paolo Puccetti

The Perspective by Pallotta et al. (1) offers the opportunity of a few more considerations on the mutually supportive relationship between tryptophan catabolic enzymes and the aryl hydrocarbon receptor (AhR) in the transitional response aimed at reinstalling homeostatic tolerance after meeting the needs of an acute inflammatory reaction (2). One major question is in fact – Why does AhR need two...

Journal: :Cancer research 1967
F W Sunderman

Administration of nickel carbonyl to rats by intravenous in jection (2 mg Ni/100 gm body weight) inhibited the induction of hepatic tryptophan pyrrolase by cortisone but not by tryptophan. Cortisone induction was impaired on the day after admin istration of nickel carbonyl. It reached a minimum at 2 days and remained diminished for 5 days. The average activity of hepatic tryptophan pyrrolase in...

2017
Paula Jouhten Jaime Huerta-Cepas Peer Bork Kiran Raosaheb Patil

Microbial cell factories based on renewable carbon sources are fundamental to a sustainable bio-economy. The economic feasibility of producer cells requires robust performance balancing growth and production. However, the inherent competition between these two objectives often leads to instability and reduces productivity. While algorithms exist to design metabolic network reduction strategies ...

Journal: :Journal of bacteriology 1968
L J Berry D S Smythe L S Colwell

Bacterial endotoxins in mice reduced the induction by cortisone of two hepatic enzymes, tryptophan oxygenase, and phosphoenolpyruvate carboxykinase, they prevented the glyconeogenesis in liver induced by the same hormone, and they induced in intact animals the liver enzyme tyrosine-alpha-ketoglutarate transaminase, all in proportion to their ld(50). When cortisone was given in the least amount ...

Journal: :The Journal of biological chemistry 1975
F O Brady P Feigelson

The oxygenated complexes of the two catalytically active forms of pseudomonad and rat liver L-tryptophan-2,3-dioxygenase (EC 1.13.11.11) have been studied. As was previously reported (ISHIMURA, Y., NORZAKI, M., HAYAISHI, O., TAMURA, M., AND YAMAZAK-I I. (1970) J. Biol. Chem. 245, 3593-3602), we observe that the fully reduced form of pseudomonad tryptophan oxygenase during steady state catalysis...

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