The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Mechanism for irreversible self-deactivation of prostaglandin synthetase.
Open accessAbstract
It has been shown that prostaglandin (PG) cyclooxygenase is irreversibly self-deactivated during the oxygenation of arachidonic acid (Smith, W. L., and Lands, W.E.M. (1972) Biochemistry II, 3273-3285). Using several experimental approaches and an enzyme preparation which was highly active without artificial stimulation, we have extensively investigated the mechanism of this deactivation process. During the generation of PGH2 from arachidonic acid, oxidizing equivalents were released and the reductive breakdown of PGG2 was found to deactivate the cyclooxygenase. The cyclooxygenase-catalyzed metabolism of both arachidonic acid and PGG2 generated radicals which were scavenged by phenol. Both phenol and methional (scavengers of oxygen-centered radicals) promoted the formation of PGH2 at the expense of PGG2 and increased the initial rate and the extent of reaction prior to deactivation of the cyclooxygenase. Hence, it appears that the cyclooxygenase was irreversibly self-deactivated during the formation of PGH2 from arachidonic acid, due to its oxidation by oxygen-centered radicals formed as a result of the reductive breakdown of the hydroperoxide on PGG2. Some experiments with dithiothereitol and N-ethylmaleimide suggested that the enzyme may contain a disulfide at the active site. A mechanism has been devised which accounts for the self-deactivation phenomenon, the effect of phenol and methional, the disulfide at the active site, and the pathway of substrate oxygenation.
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Cites
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Isolation and Structure of Two Prostaglandin Endoperoxides That Cause Platelet Aggregation
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Isolation and properties of intermediates in prostaglandin biosynthesis
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A Mechanism for the Production of Ethylene from Methional
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Detection and Isolation of an Endoperoxide Intermediate in Prostaglandin Biosynthesis
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PGH synthase and lipoxygenase generate superoxide in the presence of NADH or NADPH.
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Initiation of lipid peroxidation in biological systems
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Metadata
- Authors
- Egan, R. W., Paxton, J., & Kuehl, F. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1976-12
- Volume
- 251
- Issue
- 23
- Pages
- 7329-7335
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1638102173
- Cited by
- 586
- References
- 15
- FWCI
- 15.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Egan, R. W., Paxton, J., & Kuehl, F. A. (1976). Mechanism for irreversible self-deactivation of prostaglandin synthetase. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)32853-3
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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