NDLI: Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.

Please wait, while we are loading the content...

A thioredoxin fusion protein of VanH, a D-lactate dehydrogenase from Enterococcus faecium: cloning, expression, purification, kinetic analysis, and crystallization.

Reactivation of thermally inactivated pre-beta-lactamase by DnaK, DnaJ, and GrpE.

Topology of sarcoplasmic reticulum Ca2+-ATPase: an infrared study of thermal denaturation and limited proteolysis.

The observation of chaperone-ligand noncovalent complexes with electrospray ionization mass spectrometry.

Isolation and characterization of a DnaJ-like protein in rats: the C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like protein.

Calorimetric analyses of the interaction between SecB and its ligands.

What should the Z-score of native protein structures be?

The role of tyrosine 121 in cofactor binding of 5-aminolevulinate synthase.

Synthesis, physicochemical characterization, and crystallization of a putative retro-coiled coil.

Mutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli.

Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.

Assembly and crystallization of the complex between the human T cell coreceptor CD8alpha homodimer and HLA-A2.

Homologues of 26S proteasome subunits are regulators of transcription and translation.

Crystal structures of two mutants that have implications for the folding of bovine pancreatic ribonuclease A.

Crystallization and preliminary X-ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H-D-Phe-Phe-Arg-chloromethylketone.

Baseline length and automated fitting of denaturation data.

Production, crystallization, and preliminary X-ray analysis of the human MHC class Ib molecule HLA-E.

Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase.

Year: 1998 Volume: 7 Issue: 4

Year: 1998 Volume: 7 Issue: 3

Year: 1998 Volume: 7 Issue: 2

Year: 1998 Volume: 7 Issue: 1

Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mössner, E. Glockshuber, R. Huber-Wunderlich, M.
Description	Country affiliation: Switzerland Author Affiliation: Mössner E ( Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Hönggerberg, Zürich, Switzerland.)
Abstract	Thiol/disulfide oxidoreductases like thioredoxin, glutaredoxin, DsbA, or protein disulfide isomerase (PDI) share the thioredoxin fold and a catalytic disulfide bond with the sequence Cys-Xaa-Xaa-Cys (Xaa corresponds to any amino acid). Despite their structural similarities, the enzymes have very different redox properties, which is reflected by a 100,000-fold difference in the equilibrium constant (K(eq)) with glutathione between the most oxidizing member, DsbA, and the most reducing member, thioredoxin. Here we present a systematic study on a series of variants of thioredoxin from Escherichia coli, in which the Xaa-Xaa dipeptide was exchanged by that of glutaredoxin, PDI, and DsbA. Like the corresponding natural enzymes, all thioredoxin variants proved to be stronger oxidants than the wild-type, with the order wild-type < PDI-type < DsbA-type < glutaredoxin-type. The most oxidizing, glutaredoxin-like variant has a 420-fold decreased value of K(eq), corresponding to an increase in redox potential by 75 mV. While oxidized wild-type thioredoxin is more stable than the reduced form (delta deltaG(ox/red) = 16.9 kJ/mol), both redox forms have almost the same stability in the variants. The pH-dependence of the reactivity with the alkylating agent iodoacetamide proved to be the best method to determine the pKa value of thioredoxin's nucleophilic active-site thiol (Cys32). A pKa of 7.1 was measured for Cys32 in the reduced wild-type. All variants showed a lowered pKa of Cys32, with the lowest value of 5.9 for the glutaredoxin-like variant. A correlation of redox potential and the Cys32 pKa value could be established on a quantitative level. However, the predicted correlation between the measured delta deltaG(ox/red) values and Cys32 pKa values was only qualitative.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	7
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1998-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Escherichia Coli Metabolism Oxidoreductases Protein Disulfide Reductase (glutathione) Thioredoxins Binding Sites Circular Dichroism Cysteine Glutaredoxins Oxidation-reduction Recombinant Proteins Genetics Isolation & Purification Spectrophotometry, Ultraviolet Thermodynamics Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.

Enzymatic reduction of alloxan by thioredoxin and NADPH-thioredoxin reductase.

Thioredoxin h isoforms from rice are differentially reduced by NADPH/thioredoxin or GSH/glutaredoxin systems.

Mammalian thioredoxin reductase: oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity.

Thioredoxin, glutaredoxin, and thioredoxin reductase from cultured HeLa cells.

The crystal structure of the protein YhaK from Escherichia coli reveals a new subclass of redox sensitive enterobacterial bicupins.

Selective targeting of the cysteine proteome by thioredoxin and glutathione redox systems.

Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence.

System xc− and Thioredoxin Reductase 1 Cooperatively Rescue Glutathione Deficiency

Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.

Similar Documents

Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.

Enzymatic reduction of alloxan by thioredoxin and NADPH-thioredoxin reductase.

Thioredoxin h isoforms from rice are differentially reduced by NADPH/thioredoxin or GSH/glutaredoxin systems.

Mammalian thioredoxin reductase: oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity.

Thioredoxin, glutaredoxin, and thioredoxin reductase from cultured HeLa cells.

The crystal structure of the protein YhaK from Escherichia coli reveals a new subclass of redox sensitive enterobacterial bicupins.

Selective targeting of the cysteine proteome by thioredoxin and glutathione redox systems.

Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence.

System xc− and Thioredoxin Reductase 1 Cooperatively Rescue Glutathione Deficiency

Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.