| Autor: |
Gorina SS; Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, Russia., Iljina TM; Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, Russia., Mukhtarova LS; Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, Russia., Toporkova YY; Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, Russia., Grechkin AN; Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, P.O. Box 30, 420111 Kazan, Russia. |
| Jazyk: |
angličtina |
| Zdroj: |
International journal of molecular sciences [Int J Mol Sci] 2022 Jul 20; Vol. 23 (14). Date of Electronic Publication: 2022 Jul 20. |
| DOI: |
10.3390/ijms23148009 |
| Abstrakt: |
The genome of the neotropical fruit bat Sturnira hondurensis was recently sequenced, revealing an unexpected gene encoding a plant-like protein, CYP74C44, which shares ca. 90% sequence identity with the putative CYP74C of Populus trichocarpa . 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 4 -reduced products (Me/TMS) of 15-HPEPE and 13- and 9-hydroperoxides as (all- Z )-14-hydroxy-5,8,11-tetradecatrienoic, (9 Z )-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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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