Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat <i>Sturnira hondurensis</i>
The genome of the neotropical fruit bat <i>Sturnira hondurensis</i> was recently sequenced, revealing an unexpected gene encoding a plant-like protein, CYP74C44, which shares ca. 90% sequence identity with the putative CYP74C of <i>Populus trichocarpa</i>. The preparation and...
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MDPI AG
2022-07-01
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| Series: | International Journal of Molecular Sciences |
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| author | Svetlana S. Gorina Tatiana M. Iljina Lucia S. Mukhtarova Yana Y. Toporkova Alexander N. Grechkin |
| author_facet | Svetlana S. Gorina Tatiana M. Iljina Lucia S. Mukhtarova Yana Y. Toporkova Alexander N. Grechkin |
| author_sort | Svetlana S. Gorina |
| collection | DOAJ |
| description | The genome of the neotropical fruit bat <i>Sturnira hondurensis</i> was recently sequenced, revealing an unexpected gene encoding a plant-like protein, CYP74C44, which shares ca. 90% sequence identity with the putative CYP74C of <i>Populus trichocarpa</i>. The preparation and properties of the recombinant CYP74C44 are described in the present work. The CYP74C44 enzyme was found to be active against the 13- and 9-hydroperoxides of linoleic and α-linolenic acids (13-HPOD, 13-HPOT, 9-HPOD, and 9-HPOT, respectively), as well as the 15-hydroperoxide of eicosapentaenoic acid (15-HPEPE). All substrates studied were specifically transformed into chain cleavage products that are typical for hydroperoxide lyases (HPLs). The HPL chain cleavage reaction was validated by the identification of NaBH<sub>4</sub>-reduced products (Me/TMS) of 15-HPEPE and 13- and 9-hydroperoxides as (all-<i>Z</i>)-14-hydroxy-5,8,11-tetradecatrienoic, (9<i>Z</i>)-12-hydroxy-9-dodecenoic, and 9-hydroxynonanoic acids (Me/TMS), respectively. Thus, CYP74C44 possessed the HPL activity that is typical for the CYP74C subfamily proteins. |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T13:40:46Z |
| publishDate | 2022-07-01 |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-d2b72936c69e483883d7f5440b8abc0d2023-11-30T21:07:34ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-07-012314800910.3390/ijms23148009Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat <i>Sturnira hondurensis</i>Svetlana S. Gorina0Tatiana M. Iljina1Lucia S. Mukhtarova2Yana Y. Toporkova3Alexander N. Grechkin4Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, RussiaKazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, RussiaKazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, RussiaKazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, RussiaKazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, RussiaThe genome of the neotropical fruit bat <i>Sturnira hondurensis</i> was recently sequenced, revealing an unexpected gene encoding a plant-like protein, CYP74C44, which shares ca. 90% sequence identity with the putative CYP74C of <i>Populus trichocarpa</i>. The preparation and properties of the recombinant CYP74C44 are described in the present work. The CYP74C44 enzyme was found to be active against the 13- and 9-hydroperoxides of linoleic and α-linolenic acids (13-HPOD, 13-HPOT, 9-HPOD, and 9-HPOT, respectively), as well as the 15-hydroperoxide of eicosapentaenoic acid (15-HPEPE). All substrates studied were specifically transformed into chain cleavage products that are typical for hydroperoxide lyases (HPLs). The HPL chain cleavage reaction was validated by the identification of NaBH<sub>4</sub>-reduced products (Me/TMS) of 15-HPEPE and 13- and 9-hydroperoxides as (all-<i>Z</i>)-14-hydroxy-5,8,11-tetradecatrienoic, (9<i>Z</i>)-12-hydroxy-9-dodecenoic, and 9-hydroxynonanoic acids (Me/TMS), respectively. Thus, CYP74C44 possessed the HPL activity that is typical for the CYP74C subfamily proteins.https://www.mdpi.com/1422-0067/23/14/8009cytochrome P450CYP74hydroperoxide lyasemammalsfruit bat<i>Sturnira hondurensis</i> |
| spellingShingle | Svetlana S. Gorina Tatiana M. Iljina Lucia S. Mukhtarova Yana Y. Toporkova Alexander N. Grechkin Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat <i>Sturnira hondurensis</i> International Journal of Molecular Sciences cytochrome P450 CYP74 hydroperoxide lyase mammals fruit bat <i>Sturnira hondurensis</i> |
| title | Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat <i>Sturnira hondurensis</i> |
| title_full | Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat <i>Sturnira hondurensis</i> |
| title_fullStr | Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat <i>Sturnira hondurensis</i> |
| title_full_unstemmed | Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat <i>Sturnira hondurensis</i> |
| title_short | Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat <i>Sturnira hondurensis</i> |
| title_sort | detection of unprecedented cyp74 enzyme in mammal hydroperoxide lyase cyp74c44 of the bat i sturnira hondurensis i |
| topic | cytochrome P450 CYP74 hydroperoxide lyase mammals fruit bat <i>Sturnira hondurensis</i> |
| url | https://www.mdpi.com/1422-0067/23/14/8009 |
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