ArticleThe Journal of biological chemistry2009
Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- Molecular Analysis of Two CC-Type Glutaredoxins from the Model LegumeInternational journal of molecular sciences · 2026Article
- A universal cis-proline lock defines catalysis in thioredoxin-fold enzymes.Communications biology · 2026Article
- Structural and Biophysical Analyses of Human Prostamide/Prostaglandin F Synthase with Two Active Form-Mimicking Mutations.Biomolecules · 2026Article
- Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding.Protein science : a publication of the Protein Society · 2026Article
- Identification and functional characterization of a novel thioredoxin MpTRX1 from Metschnikowia persimmonesis.Applied microbiology and biotechnology · 2025Article
- Oxidative Stress and Antioxidants in Glioblastoma: Mechanisms of Action, Therapeutic Effects and Future Directions.Antioxidants (Basel, Switzerland) · 2025Review
- Aromatic Residue Variations in the Central β‑Sheet Influence Stability and Activity of E. coli Glutaredoxin 3.ACS omega · 2025Article
- Unveiling the versatility of the thioredoxin framework: Insights from the structural examination ofComputational and structural biotechnology journal · 2024Article
- Glutathione and Glutaredoxin-Key Players in Cellular Redox Homeostasis and Signaling.Antioxidants (Basel, Switzerland) · 2023Review
- Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat-labile structure from the Arctic bacterium Sphingomonas sp.FEBS open bio · 2023Article
- AC81 Is a Putative Disulfide Isomerase Involved in Baculoviral Disulfide Bond Formation.Journal of virology · 2022Article
- Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases ofInternational journal of molecular sciences · 2021Article
- Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates.Computational and structural biotechnology journal · 2021Review
- Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease.International journal of molecular sciences · 2020Review
- Deciphering the Role of Multiple Thioredoxin Fold Proteins ofInternational journal of molecular sciences · 2020Article
- C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning.PloS one · 2020Article
- Impact of key residues within chloroplast thioredoxin-The Journal of biological chemistry · 2019Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Two DsbA Proteins Are Important forFrontiers in microbiology · 2019Article
- Characterization of TrxC, an Atypical Thioredoxin Exclusively Present in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2018Article
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adjacent in three-dimensional space to the characteristic CXXC active site motif of thioredoxin fold proteins but distant in sequence. This residue is just N-terminal to the conservative cis-proline. It is isoleucine 75 in the case of thioredoxin. Our findings support the conclusion that a very small percentage of the amino acid residues of thioredoxin-related proteins are capable of dictating the functions of these proteins.
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