A Reexamination of Thioredoxin Reductase from Thermoplasma acidophilum, a Thermoacidophilic Euryarchaeon, Identifies It as an NADH-Dependent Enzyme

Isoprenoids are a large class of natural products with wide-ranging applications. Synthetic biology approaches to the manufacture of isoprenoids and their new-to-nature derivatives are limited due to the provision in Nature of just two hemiterpene building blocks for isoprenoid biosynthesis. To address this limitation, artificial chemo-enzymatic pathways such as the alcohol-dependent hemiterpene pathway (ADH) serve to leverage consecutive kinases to convert exogenous alcohols to pyrophosphates that could be coupled to downstream isoprenoid biosynthesis. To be successful, each kinase in this pathway should be permissive of a broad range of substrates. For the first time, we have probed the promiscuity of the second enzyme in the ADH pathway, isopentenyl phosphate kinase from Thermoplasma acidophilum, towards a broad range of acceptor monophosphates. Subsequently, we evaluate the suitability of this enzyme to provide non-natural pyrophosphates and provide a critical first step in characterizing the rate limiting steps in the artificial ADH pathway.<br>

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Faculty Opinions recommendation of Selenite assimilation into formate dehydrogenase H depends on thioredoxin reductase in Escherichia coli.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1104860.560947 ◽

2008 ◽

Author(s):

Russ Hille

Keyword(s):

Escherichia Coli ◽

Formate Dehydrogenase ◽

Thioredoxin Reductase

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Faculty Opinions recommendation of The thioredoxin reductase-glutaredoxins-ferredoxin crossroad pathway for selenate tolerance in Synechocystis PCC6803.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1147965.605064 ◽

2009 ◽

Author(s):

Tamar Barkay

Keyword(s):

Thioredoxin Reductase ◽

Synechocystis Pcc6803

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Computational Approaches as Rational Decision Support Systems for Discovering Next-Generation Antitubercular Agents: Mini-Review

Current Computer - Aided Drug Design ◽

10.2174/1573409915666190130153214 ◽

2019 ◽

Vol 15 (5) ◽

pp. 369-383

Author(s):

Rahul Balasaheb Aher ◽

Kunal Roy

Keyword(s):

Recent Progress ◽

Neglected Tropical Diseases ◽

Acyl Carrier Protein ◽

Thioredoxin Reductase ◽

Protein Tyrosine Phosphatases ◽

Antitubercular Agents ◽

Computer Aided Drug Design ◽

Modeling Studies ◽

Catalase Peroxidase ◽

Molecular Modeling Studies

Tuberculosis, malaria, dengue, chikungunya, leishmaniasis etc. are a large group of neglected tropical diseases that prevail in tropical and subtropical countries, affecting one billion people every year. Minimal funding and grants for research on these scientific problems challenge many researchers to find a different way to reduce the extensive time and cost involved in the drug discovery cycle of these problems. Computer-aided drug design techniques have already been proved successful in the discovery of new molecules rationally by reducing the time and cost involved in the development of drugs. In the current minireview, we are highlighting on the molecular modeling studies published during 2010-2018 for target specific antitubercular agents. This review includes the studies of Structure-Based (SB) and Ligand-Based (LB) modeling and those involving Machine Learning (ML) techniques against different antitubercular targets such as dihydrofolate reductase (DHFR), enoyl Acyl Carrier Protein (ACP) reductase (InhA), catalase-peroxidase (KatG), enzyme antigen 85C, protein tyrosine phosphatases (PtpA and PtpB), dUTPase, thioredoxin reductase (MtTrxR), etc. The information presented in this review will help the researchers to get acquainted with the recent progress in the modeling studies of antitubercular agents.

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Characterization of the Active Center of Thioredoxin Reductase

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)99416-0 ◽

1967 ◽

Vol 242 (22) ◽

pp. 5232-5236 ◽

Cited By ~ 1

Author(s):

Giuliana Zanetti ◽

Charles H. Williams

Keyword(s):

Active Center ◽

Thioredoxin Reductase

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Pap1p-dependent upregulation of thioredoxin 3 and thioredoxin reductase genes from the fission yeast under nitrosative stress

Canadian Journal of Microbiology ◽

10.1139/w11-125 ◽

2012 ◽

Vol 58 (2) ◽

pp. 206-211 ◽

Cited By ~ 3

Author(s):

Min-Sik Park ◽

Hyeon-Jung Kim ◽

A Rum Park ◽

Kisup Ahn ◽

Hye-Won Lim ◽

...

Keyword(s):

Fission Yeast ◽

Nitrosative Stress ◽

Thioredoxin Reductase

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System-wide identification and prioritization of enzyme substrates by thermal analysis

Nature Communications ◽

10.1038/s41467-021-21540-6 ◽

2021 ◽

Vol 12 (1) ◽

Author(s):

Amir Ata Saei ◽

Christian M. Beusch ◽

Pierre Sabatier ◽

Juan Astorga Wells ◽

Hassan Gharibi ◽

...

Keyword(s):

Thermal Analysis ◽

Thioredoxin Reductase ◽

Structural Level ◽

Post Translational Modification ◽

Post Translational Modifications ◽

Enzyme Substrate ◽

Thioredoxin Reductase 1 ◽

Enzyme Substrates ◽

Substrate Proteins

AbstractDespite the immense importance of enzyme–substrate reactions, there is a lack of general and unbiased tools for identifying and prioritizing substrate proteins that are modified by the enzyme on the structural level. Here we describe a high-throughput unbiased proteomics method called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA). The approach assumes that the enzymatic post-translational modification of substrate proteins is likely to change their thermal stability. In our proof-of-concept studies, SIESTA successfully identifies several known and novel substrate candidates for selenoprotein thioredoxin reductase 1, protein kinase B (AKT1) and poly-(ADP-ribose) polymerase-10 systems. Wider application of SIESTA can enhance our understanding of the role of enzymes in homeostasis and disease, opening opportunities to investigate the effect of post-translational modifications on signal transduction and facilitate drug discovery.

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