A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an enzyme with protein disulfide reductase activity

FEBS Letters ◽  
2009 ◽  
Vol 583 (9) ◽  
pp. 1399-1402 ◽  
Author(s):  
Juan Manuel Pérez-Ruiz ◽  
Francisco Javier Cejudo
Keyword(s):  
Reaction Mechanism ◽  
Reductase Activity ◽  
Thioredoxin Reductase ◽  
Disulfide Reductase ◽  
Protein Disulfide

scholarly journals The Archaeon Methanosarcina acetivorans Contains a Protein Disulfide Reductase with an Iron-Sulfur Cluster

2007 ◽  
Vol 189 (20) ◽  
pp. 7475-7484 ◽  
Author(s):  
Daniel J. Lessner ◽  
James G. Ferry
Keyword(s):  
Aromatic Compounds ◽  
Stress Proteins ◽  
Reductase Activity ◽  
Strictly Anaerobic ◽  
Methanosarcina Acetivorans ◽  
Gene Encoding ◽  
Iron Sulfur Cluster ◽  
Disulfide Reductase ◽  
Regulate Protein ◽  
Protein Disulfide

ABSTRACT Methanosarcina acetivorans, a strictly anaerobic methane-producing species belonging to the domain Archaea, contains a gene cluster annotated with homologs encoding oxidative stress proteins. One of the genes (MA3736) is annotated as a gene encoding an uncharacterized carboxymuconolactone decarboxylase, an enzyme required for aerobic growth with aromatic compounds by species in the domain Bacteria. Methane-producing species are not known to utilize aromatic compounds, suggesting that MA3736 is incorrectly annotated. The product of MA3736, overproduced in Escherichia coli, had protein disulfide reductase activity dependent on a C67XXC70 motif not found in carboxymuconolactone decarboxylase. We propose that MA3736 be renamed mdrA (methanosarcina disulfide reductase). Further, unlike carboxymuconolactone decarboxylase, MdrA contained an Fe-S cluster. Binding of the Fe-S cluster was dependent on essential cysteines C67 and C70, while cysteines C39 and C107 were not required. Loss of the Fe-S cluster resulted in conversion of MdrA from an inactive hexamer to a trimer with protein disulfide reductase activity. The data suggest that MdrA is the prototype of a previously unrecognized protein disulfide reductase family which contains an intermolecular Fe-S cluster that controls oligomerization as a mechanism to regulate protein disulfide reductase activity.

scholarly journals Identification of Multiple Soluble Fe(III) Reductases in Gram-Positive Thermophilic BacteriumThermoanaerobacter indiensisBSB-33

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Subrata Pal
Keyword(s):  
Reductase Activity ◽  
Three Dimensional ◽  
Thioredoxin Reductase ◽  
Desulfovibrio Desulfuricans ◽  
Structural Similarity ◽  
Thermophilic Bacterium ◽  
Gram Positive ◽  
Reduction Activity ◽  
Structural Identity ◽  
Disulfide Reductase

Thermoanaerobacter indiensisBSB-33 has been earlier shown to reduce Fe(III) and Cr(VI) anaerobically at 60°C optimally. Further, the Gram-positive thermophilic bacterium contains Cr(VI) reduction activity in both the membrane and cytoplasm. The soluble fraction prepared fromT. indiensiscells grown at 60°C was found to contain the majority of Fe(III) reduction activity of the microorganism and produced four distinct bands in nondenaturing Fe(III) reductase activity gel. Proteins from each of these bands were partially purified by chromatography and identified by mass spectrometry (MS) with the help ofT. indiensisproteome sequences. Two paralogous dihydrolipoamide dehydrogenases (LPDs), thioredoxin reductase (Trx), NADP(H)-nitrite reductase (Ntr), and thioredoxin disulfide reductase (Tdr) were determined to be responsible for Fe(III) reductase activity. Amino acid sequence and three-dimensional (3D) structural similarity analyses of theT. indiensisFe(III) reductases were carried out with Cr(VI) reducing proteins from other bacteria. The two LPDs and Tdr showed very significant sequence and structural identity, respectively, with Cr(VI) reducing dihydrolipoamide dehydrogenase fromThermus scotoductusand thioredoxin disulfide reductase fromDesulfovibrio desulfuricans. It appears that in addition to their iron reducing activityT. indiensisLPDs and Tdr are possibly involved in Cr(VI) reduction as well.

Structural and Biochemical Characterizations of Methanoredoxin fromMethanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity

Biochemistry ◽  
2015 ◽  
Vol 55 (2) ◽  
pp. 313-321 ◽  
Author(s):  
Deepa Yenugudhati ◽  
Divya Prakash ◽  
Adepu K. Kumar ◽  
R. Siva Sai Kumar ◽  
Neela H. Yennawar ◽  
...  
Keyword(s):  
Reductase Activity ◽  
Coenzyme M ◽  
Disulfide Reductase ◽  
Dependent Protein ◽  
Protein Disulfide

Thioredoxin liquefies and decreases the viscoelasticity of cystic fibrosis sputum

2004 ◽  
Vol 286 (5) ◽  
pp. L931-L938 ◽  
Author(s):  
Raymond C. Rancourt ◽  
Shusheng Tai ◽  
Malcolm King ◽  
Sonya L. Heltshe ◽  
Churee Penvari ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Molecular Weight ◽  
Liquid Phase ◽  
Thioredoxin Reductase ◽  
Extracellular Dna ◽  
Cystic Fibrosis Sputum ◽  
Enzymatic Reduction ◽  
Disulfide Reductase ◽  
Gel Phase ◽  
Protein Disulfide

The persistent and viscous nature of airway secretions in cystic fibrosis (CF) disease leads to airway obstruction, opportunistic infection, and deterioration of lung function. Thioredoxin (Trx) is a protein disulfide reductase that catalyzes numerous thiol-dependent cellular reductive processes. To determine whether Trx can alter the rheological properties of mucus, sputum obtained from CF patients was treated with TRX and its reducing system (0.1 μM thioredoxin reductase + 2 mM NADPH), and liquid phase-gel phase ratio (percent liquid phase) was assessed by compaction assay. Exposure to low Trx concentrations (1 μM) caused significant increases in the percentage of liquid phase of sputum. Maximal increases in percent liquid phase occurred with 30 μM Trx. Additional measurements revealed that sputum liquefaction by the Trx reducing system is dependent on NADPH concentration. The relative potency of the Trx reducing system also was compared with other disulfide-reducing agents. In contrast with Trx, glutathione and N-acetylcysteine were ineffective in liquefying sputum when used at concentrations <1 mM. Sputum viscoelasticity, measured by magnetic microrheometry, also was diminished significantly following 20-min treatment with 3, 10, or 30 μM Trx. Similarly, this reduction in viscoelasticty also was dependent on NADPH concentration. Further investigation has indicated that Trx treatment increases the solubility of high-molecular-weight glycoproteins and causes redistribution of extracellular DNA into the liquid phase of sputum. Recognizing that mucins are the major gel-forming glycoproteins in mucus, we suggest that Trx alters sputum rheology by enzymatic reduction of glycoprotein polymers present in sputum.

NADPH-Dependent Thioredoxin Reductase and a New Thioredoxin from Wheat

1979 ◽  
Vol 34 (3-4) ◽  
pp. 214-221 ◽  
Author(s):  
Guntram Suske ◽  
Wolfgang Wagner ◽  
Hartmut Follmann
Keyword(s):  
Gel Filtration ◽  
Deae Cellulose ◽  
Plant Cells ◽  
Thioredoxin Reductase ◽  
E Coli ◽  
Heat Stable ◽  
Thioredoxin System ◽  
Disulfide Reductase ◽  
Germinating Seeds ◽  
Protein Disulfide

Abstract An album in fraction extracted from wheat flour contains thioredoxin reductase (Mr = 65,000) and a heat-stable thioredoxin (Mr = 15,000) which are separated on DEAE cellulose and further purified by gel filtration. W heat thioredoxin stimulates E. coli ribonucleotide reductase but not chloroplast fructose-bis-phosphatase. The enzyme is NADPH -dependent (Km = 3.2 X 10-6 ᴍ) . In presence of the thioredoxin it slowly reduces other proteins like insulin or ribonuclease. Therefore it is most likely identical with a protein disulfide reductase (of unknown specificity) previously described in wheat. This new thioredoxin system is a counterpart of the ferredoxin-dependent system found in photosynthetic plant cells, suggesting different, specific mechanisms for regeneration of reduced thioredoxins in germinating seeds and green plants.

scholarly journals Fluorogenic probes for thioredoxin reductase activity

2021 ◽  
Vol 3 ◽  
pp. 100127
Author(s):  
Tendai J. Mafireyi ◽  
Jorge O. Escobedo ◽  
Robert M. Strongin
Keyword(s):  
Reductase Activity ◽  
Thioredoxin Reductase ◽  
Fluorogenic Probes

scholarly journals Structural Basis of an ERAD Pathway Mediated by the ER-Resident Protein Disulfide Reductase ERdj5

2011 ◽  
Vol 41 (4) ◽  
pp. 432-444 ◽  
Author(s):  
Masatoshi Hagiwara ◽  
Ken-ichi Maegawa ◽  
Mamoru Suzuki ◽  
Ryo Ushioda ◽  
Kazutaka Araki ◽  
...  
Keyword(s):  
Structural Basis ◽  
Disulfide Reductase ◽  
Protein Disulfide ◽  
Erad Pathway

scholarly journals Mitochondrial Thioredoxin-Glutathione Reductase from LarvalTaenia crassiceps(Cysticerci)

2010 ◽  
Vol 2010 ◽  
pp. 1-11 ◽  
Author(s):  
Alberto Guevara-Flores ◽  
Irene P. del Arenal ◽  
Guillermo Mendoza-Hernández ◽  
Juan Pablo Pardo ◽  
Oscar Flores-Herrera ◽  
...  
Keyword(s):  
Glutathione Reductase ◽  
Reductase Activity ◽  
Catalytic Efficiency ◽  
Dependent Manner ◽  
Exchange Reactions ◽  
Disulfide Exchange ◽  
Oxidative Inactivation ◽  
Disulfide Reductase ◽  
Thioredoxin Peroxidase ◽  
Thioredoxin Glutathione Reductase

Mitochondrial thioredoxin-glutathione reductase was purified from larvalTaenia crassiceps(cysticerci). The preparation showed NADPH-dependent reductase activity with either thioredoxin or GSSG, and was able to perform thiol/disulfide exchange reactions. At25∘Cspecific activities were437  ±  27mU mg-1and840  ±  49mU mg-1with thioredoxin and GSSG, respectively. ApparentKmvalues were0.87  ±  0.04 μM,41  ±  6 μM and19  ±  10 μM for thioredoxin, GSSG and NADPH, respectively. Thioredoxin from eukaryotic sources was accepted as substrate. The enzyme reduced H2O2in a NADPH-dependent manner, although with low catalytic efficiency. In the presence of thioredoxin, mitochondrial TGR showed a thioredoxin peroxidase-like activity. All disulfide reductase activities were inhibited by auranofin, suggesting mTGR is dependent on selenocysteine. The reductase activity with GSSG showed a higher dependence on temperature as compared with the DTNB reductase activity. The variation of the GSSG- and DTNB reductase activities on pH was dependent on the disulfide substrate. Like the cytosolic isoform, mTGR showed a hysteretic kinetic behavior at moderate or high GSSG concentrations, but it was less sensitive to calcium. The enzyme was able to protect glutamine synthetase from oxidative inactivation, suggesting that mTGR is competent to contend with oxidative stress.

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