دورية أكاديمية
Mechanism of oxygen transfer by prostaglandin hydroperoxidase.
| العنوان: | Mechanism of oxygen transfer by prostaglandin hydroperoxidase. |
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| المؤلفون: | Egan RW, Gale PH, VandenHeuvel WJ, Baptista EM, Kuehl FA Jr |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 1980 Jan 25; Vol. 255 (2), pp. 323-6. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Microsomes/*enzymology , Peroxidases/*metabolism , Seminal Vesicles/*enzymology, Animals ; Indomethacin/pharmacology ; Kinetics ; Male ; Mass Spectrometry ; Oxygen ; Prostaglandin Endoperoxides ; Sheep |
| مستخلص: | The peroxidase associated with prostaglandin cyclooxygenase in ram seminal vesicle microsomes will utilize a wide variety of hydroperoxides and reducing substrates. One such reducing substrate, sulindac sulfide (cis-5-fluoro-2-methyl-1-[p-(methylthio)benzylidenyl]indene-3-acetic acid), inhibits the oxygenase, stimulates the peroxidase, and is oxidized to its analogous sulfoxide by the peroxidase. The peroxidase-catalyzed transfer of oxygen atoms from 15-hydroperoxyprostaglandin E2 (15-HPE2) to sulindac sulfide was examined using [18O]15-HPE2 which was prepared enzymatically and analyzed mass spectrometrically. The sulfoxide resulting from sulindac sulfide oxidation was also analyzed mass spectrometrically and found to possess an oxygen atom arising exclusively from the 15-HPE2. Since sulindac sulfide inhibits the oxygenase activity of this enzyme (ID50 approximately equal to 0.2 microM), it seemed possible that the oxygen atom was transferred while the sulfide was bound to this site. However, indomethacin, an inhibitor of the oxygenase with no effect on the peroxidase, did not alter the stoichiometry of sulindac sulfide oxidation, precluding this possibility. These findings are discussed in the context of identifying the nature of the actual oxidant and distinguishing between the oxidation mechanisms of various peroxidases and between sulindac sulfide and other reducing substrates for these enzymes. |
| المشرفين على المادة: | 0 (Prostaglandin Endoperoxides) EC 1.11.- (prostaglandin hydroperoxidase) EC 1.11.1.- (Peroxidases) S88TT14065 (Oxygen) XXE1CET956 (Indomethacin) |
| تواريخ الأحداث: | Date Created: 19800125 Date Completed: 19800324 Latest Revision: 20210210 |
| رمز التحديث: | 20221213 |
| PMID: | 7356613 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0021-9258 |
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