نتایج جستجو برای: thioredoxin reductase

تعداد نتایج: 48195  

2017
Nicklas Skjoldager Maria Blanner Bang Martin Rykær Olof Björnberg Michael J. Davies Birte Svensson Pernille Harris Per Hägglund

The NADPH-dependent homodimeric flavoenzyme thioredoxin reductase (TrxR) provides reducing equivalents to thioredoxin, a key regulator of various cellular redox processes. Crystal structures of photo-inactivated thioredoxin reductase (TrxR) from the Gram-positive bacterium Lactococcus lactis have been determined. These structures reveal novel molecular features that provide further insight into...

Journal: :EMBO reports 2003
Eleanor W Trotter Chris M Grant

Our studies in yeast show that there is an essential requirement for either an active thioredoxin or an active glutathione (GSH)-glutaredoxin system for cell viability. Glutathione reductase (Glr1) and thioredoxin reductase (Trr1) are key regulatory enzymes that determine the redox state of the GSH-glutaredoxin and thioredoxin systems, respectively. Here we show that Trr1 is required during nor...

2013
Petra Langlotz Wolfgang Wagner Hartmut Follmann

Petra Langlotz, Wolfgang Wagner, and Hartmut Follmann Fachbereich Chemie der Philipps-Universität, Biochemie, Hans-Meerwein-Straße. D-3550 Marburg, Bundesrepublik Deutschland Z. Naturforsch. 41c, 979—987 (1986); received August 1/September 19, 1986 Am ino Acid Composition, A lgae, Ribonucleotide Reductase, Scenedesmus obliquus, Thio­ redoxin A comprehensive thioredoxin profile of Scenedesmus ob...

Journal: :Cancer research 1996
G Spyrou M Björnstedt S Skog A Holmgren

Selenium compounds like selenite and selenate have strong inhibitory effects, particularly on mammalian tumor cell growth by unknown mechanisms. We found that the addition of sodium selenite and sodium selenate inhibited the growth of human 3B6 and BL41 lymphocytes. Selenite was more potent because 10 microM selenite produced a growth inhibitory effect similar to that of 250 microM selenate. Th...

2016
Prasanta Kumar K. Mishra R. Parvathy Sunil K. Dixit Manoj Kumawat

Thioredoxin reductase (TrxB) is a flavoprotein which acts as an integral part of Thioredoxin (Trx) system. This Trx system produces reducing equivalent in various oxidation-reduction reaction which ultimately targets in various metabolic processes inside cell. TrxB must be playing role in combating various stress conditions confronted by Salmonella Typhimurium (ST) inside its host. The aim was ...

Journal: :Europan journal of science and technology 2023

Thioredoxin reductase (TrxR) is an enzyme that involved in many metabolic pathways from detoxification to reduction of radicals by catalyzing the thioredoxin, and therefore associated with physiological processes, including cancer. Inhibitors this are considered anticancer targets. In past studies, some antidepressants have been found effects through various mechanisms, reuse as drugs has attra...

Journal: :Biochimica et biophysica acta 2009
Zhenyi Zhang Rui Bao Yaru Zhang Jiang Yu Cong-Zhao Zhou Yuxing Chen

Thioredoxin reductase (TrxR) is a member of the pyridine nucleotide-disulfide oxidoreductase family of the flavoenzymes. It can use a dithiol-disulfide active-site to transfer reducing equivalents from NADPH to thioredoxin (Trx), via the cofactor FAD. In Saccharomyces cerevisiae, the cytoplasmic thioredoxin reductase Trr1 plays an important role in multiple cellular events under the control of ...

2005
ROBERT W. GEE RICHARD U. BYERRUM DENNIS W. GERBER N. E. TOLBERT

on either DEAE cellulose or Sephacryl S-200. About 80% of the reductase was one form in the chloroplast and the rest was a second form in the cytosol as determined by chromatography and by fractionation of subcellular organelles. The amount of activity detectable in the chloroplast fraction was 10.7 micromoles of dihydroxyacetone phosphate reductase per hour per milligram chlorophyll from spina...

Journal: :Journal of Biological Chemistry 1994

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