The oxidative inactivation of human alpha-1-proteinase inhibitor. Further evidence for methionine at the reactive center.
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A1AT potency is entirely abrogated under oxidative conditions due to oxidation of a methionine residue in the P1 position of its protease binding surface.
“However, the potency of A1AT inhibition is entirely abrogated under oxidative conditions, such as those induced by a neutrophil response to infection, due to the oxidation of a methionine residue in the P1 position (Schechter–Berger nomenclature [13]) of its protease binding surface [14,15].”
From Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase (2021) · cites this paper as [14]
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Persistent oxidative stress in cancer
Toyokuni, S., Okamoto, K., Yodoi, J., & Hiai, H. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01368-b · Cited by 1,219 · see citing works
The physiological role of reversible methionine oxidation
Drazic, A., & Winter, J. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.01.001 · Cited by 198 · see citing works
Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase
Leahy, D., Grant, C., Jackson, A., Duff, A., Tardiota, N., Van Haeften, J., Chen, X., Peake, J. M., Kruppa, M. D., Smith, E. T., et al. (2021) · Molecules · doi:10.3390/molecules26175344 · Cited by 2 · see citing works
“However, the potency of A1AT inhibition is entirely abrogated under oxidative conditions, such as those induced by a neutrophil response to infection, due to the oxidation of a methionine residue in the P1 position (Schechter–Berger nomenclature [13]) of its protease binding surface [14,15].”
BackgroundSelf-citation
- Authors
- Johnson, D., & Travis, J.
- Affiliations
- University of Georgia (US)
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1979-05
- Volume
- 254
- Issue
- 10
- Pages
- 4022-4026
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1583152769
- Cited by
- 466
- References
- 0
- Citations by year
- 2024: 1 · 2023: 1 · 2022: 5 · 2021: 7 · 2020: 6 · 2019: 3 · 2018: 5 · 2017: 5 · 2016: 3 · 2015: 8 · 2014: 4 · 2013: 13 · 2012: 10
- FWCI
- 11.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- alpha 1-proteinase inhibitor, oxidative inactivation, methionine, reactive centers, protein oxidation, protease inhibitors
- MeSH terms
- alpha 1-Antitrypsin, Amino Acids, Binding Sites, Chymotrypsin, Humans, Kinetics, Methionine, Oxidation-Reduction, Pancreatic Elastase, Trypsin Inhibitors
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