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Proposed Mechanism for Monomethylarsonate Reductase Activity of Human Omega-class Glutathione Transferase GSTO1
Open accessPreprint — published as 10.1016/j.bbrc.2021.12.072 · Paper page
Abstract
Contamination of drinking water with toxic inorganic arsenic is a major public health issue. The mechanisms of enzymes and transporters in arsenic elimination are therefore of interest. The human omega-class glutathione transferases have been previously shown to possess monomethylarsonate (V) reductase activity. To further understanding of this activity, molecular dynamics of human GSTO1-1 bound to glutathione with a monomethylarsonate isostere were simulated to reveal putative monomethylarsonate binding sites on the enzyme. The major binding site is in the active site, adjacent to the glutathione binding site. Based on this and previously reported biochemical data, a reaction mechanism for this enzyme is proposed. Further insights were gained from comparison of the human omega-class GSTs to homologs from a range of animals.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Oakley, A. J.
- Affiliations
- University of Wollongong (AU)
- Corresponding author
- Oakley, Aaron J
- ORCID
- Oakley, Aaron J
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- openRxiv
- Published
- 2021-11-08
- Volume
- 590
- Pages
- 7-13
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W4225861523
- Cited by
- 3
- References
- 1
- Citations by year
- 2025: 2 · 2022: 1
- FWCI
- 0.08
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Research Online (University of Wollongong) (submittedVersion)
- Figshare (submittedVersion)
- Funders
- National Institutes of Health
- University of California, San Francisco (R01-GM129325)
- Medical Research Council
- National Health and Medical Research Council (1124673, 1156455)
- National Institute of General Medical Sciences (R01GM129325)
- National Institute of Allergy and Infectious Diseases
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Physical Sciences › Environmental Science › Environmental Chemistry › Arsenic contamination and mitigation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- arsenic detoxification, inorganic arsenic, glutathione binding site, enzyme mechanism, molecular dynamics simulation, active site
- MeSH terms
- Amino Acid Sequence, Glutathione Transferase, Humans, Models, Molecular, Oxidoreductases, Catalytic Domain
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