The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Phospholipid Hydroperoxides Are Substrates for Non-selenium Glutathione Peroxidase
Open accessAbstract
This study investigated phospholipid hydroperoxides as substrates for non-selenium GSH peroxidase (NSGPx), an enzyme also called 1-Cys peroxiredoxin. Recombinant human NSGPx expressed in Escherichia coli from a human cDNA clone (HA0683) showed GSH peroxidase activity with sn-2-linolenoyl- or sn-2-arachidonoyl-phosphatidylcholine hydroperoxides as substrate; NADPH or thioredoxin could not substitute for GSH. Activity did not saturate with GSH, and kinetics were compatible with a ping-pong mechanism; kinetic constants (mM(-1) min(-1)) were k(1) = 1-3 x 10(5) and k(2) = 4-11 x 10(4). In the presence of 0.36 mM GSH, apparent K(m) was 120-130 microM and apparent V(max) was 1.5-1.6 micromol/min/mg of protein. Assays with H(2)O(2) and organic hydroperoxides as substrate indicated activity similar to that with phospholipid hydroperoxides. Maximal enzymatic activity was at pH 7-8. Activity with phospholipid hydroperoxide substrate was inhibited noncompetitively by mercaptosuccinate with K(i) 4 miroM. The enzyme had no GSH S-transferase activity. Bovine cDNA encoding NSGPx, isolated from a lung expression library using a polymerase chain reaction probe, showed >95% similarity to previously published human, rat, and mouse sequences and does not contain the TGA stop codon, which is translated as selenocysteine in selenium-containing peroxidases. The molecular mass of bovine NSGPx deduced from the cDNA is 25,047 Da. These results identify a new GSH peroxidase that is not a selenoenzyme and can reduce phospholipid hydroperoxides. Thus, this enzyme may be an important component of cellular antioxidant defense systems.
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Cited by
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Signaling Functions of Reactive Oxygen Species
Forman, H. J., Maiorino, M., & Ursini, F. (2010) · Biochemistry · doi:10.1021/bi9020378 · Cited by 827
Singlet Molecular Oxygen Reactions with Nucleic Acids, Lipids, and Proteins
Di Mascio, P., Martinez, G. R., Miyamoto, S., Ronsein, G. E., Medeiros, M. H. G., & Cadet, J. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00554 · Cited by 659
Rhee, S. G., & Woo, H. A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3393 · Cited by 463
Metadata
- Authors
- Fisher, A. B., Dodia, C., Manevich, Y., Chen, J.-W., & Feinstein, S. I.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-07
- Volume
- 274
- Issue
- 30
- Pages
- 21326-21334
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2016241657
- Cited by
- 295
- References
- 24
- FWCI
- 4.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Fisher, A. B., Dodia, C., Manevich, Y., Chen, J.-W., & Feinstein, S. I. (1999). Phospholipid Hydroperoxides Are Substrates for Non-selenium Glutathione Peroxidase. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.30.21326
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