Epoxyalcohol synthase activity of the CYP74B enzymes of higher plants

Toporkova, Yana Y.; Askarova, Elena K.; Gorina, Svetlana S.; Ogorodnikova, Anna V.; Mukhtarova, Lucia S.; Grechkin, Alexander N.

doi:10.1016/j.bbalip.2020.158743

Cited by 12 publications

(18 citation statements)

References 45 publications

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“…The GC–MS analyses of 9-HPOT and 9-HPOD products (Me/TMS) revealed compound 4a , which exhibited the following mass spectral patterns: M + at m / z 186 (0.03%), [M–C=O] + at m / z 158 (8%), [M–MeOH] + at m / z 155 (16%), [M–CH 2 CH=O] + at m / z 143 (16%), m / z 111 (56%), m / z 87 (74%), m / z 83 (60%), m / z 74 (100%), and m / z 69 (31%). The spectrum matched that for 9-oxononanoic acid (Me) [ 11 ]. Analyses of NaBH 4 -reduced 9-HPOT and 9-HPOD products (Me/TMS) showed a predominance of the single product 4 , possessing the following mass fragmentation patterns: [M–H] + at m / z 259 (0.1%), [M–Me] + at m / z 245 (20%), [245–MeOH] + at m / z 213 (100%), m / z 195 (4%), m / z 171 (6%), [CH 2 =O + –SiMe 3 ] at m / z 103 (29%), m / z 89 (35%), m / z 75 (47%), and [SiMe 3 ] + at m / z 73 (56%).…”

Section: Resultsmentioning

confidence: 62%

“…The mass spectrum of this NaBH 4 -reduced product (Me/TMS) possessed the following diagnostic and prominent fragments: [M–Me] + at m / z 285 (1%), [M–CH 2 OTMS + TMS] + at m / z 270 (5%), [285–MeOH] + at m / z 253 (6%), [M–TMSOH] + at m / z 210 (5%), [210–MeOH] + at m / z 178 (13%), m / z 159 (12%), m / z 123 (31%), [CH 2 =O + –SiMe 3 ] at m / z 103 (100%), and [SiMe 3 ] + at m / z 73 (86%). The spectrum of compound 1 matched that for (9 Z )-12-hydroxy-9-dodecenoic acid (Me/TMS) [ 11 ]. The next eluting smaller peak for 2 with a retention time of 10.3 min possessed similar spectral patterns: M + at m / z 300 (0.6%), [M–Me] + at m / z 285 (2%), [285–MeOH] + at m / z 253 (13%), m / z 185 (4%), m / z 159 (8%), m / z 143 (12%), m / z 129 (64%), m / z 75 (47%), and [SiMe 3 ] + at m / z 73 (100%).…”

Section: Resultsmentioning

confidence: 92%

“…The next eluting smaller peak for 2 with a retention time of 10.3 min possessed similar spectral patterns: M + at m / z 300 (0.6%), [M–Me] + at m / z 285 (2%), [285–MeOH] + at m / z 253 (13%), m / z 185 (4%), m / z 159 (8%), m / z 143 (12%), m / z 129 (64%), m / z 75 (47%), and [SiMe 3 ] + at m / z 73 (100%). The spectrum of product 2 corresponded to that for (10 E )-12-hydroxy-10-dodecenoic acid (Me/TMS) [ 11 ]. Catalytic hydrogenation of both compounds 1 and 2 (Me esters) followed by trimethylsilylation resulted in the product 3 (Me/TMS), whose mass spectrum possessed M + at m / z 302 (0.6%), [M–Me] + at m / z 287 (15%), [287–MeOH] + at m / z 255 (100%), m / z 204 (28%), m / z 191 (12%), m / z 107 (20%), [CH 2 =O + –SiMe 3 ] at m / z 103 (22%), m / z 75 (48%), and [SiMe 3 ] + at m / z 73 (62%).…”

Section: Resultsmentioning

confidence: 99%

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Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat Sturnira hondurensis

Gorina

Iljina

Mukhtarova

et al. 2022

IJMS

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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 NaBH4-reduced products (Me/TMS) of 15-HPEPE and 13- and 9-hydroperoxides as (all-Z)-14-hydroxy-5,8,11-tetradecatrienoic, (9Z)-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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Section: Resultsmentioning

confidence: 62%

Section: Resultsmentioning

confidence: 92%

Section: Resultsmentioning

confidence: 99%

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Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat Sturnira hondurensis

Gorina

Iljina

Mukhtarova

et al. 2022

IJMS

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“…Presumably, the presence of ω3 double bond facilitates the elimination of hydrogen at the oxirane to form allene oxide. Similarly, the LuDES (CYP74B16) dehydrates the 13-HPOT predominantly to divinyl ether (ω5Z)-etherolenic acid, while 13-HPOD is largely isomerized to the hemiacetal (the HPL product) [ 29 ]. These observations indicate that the ω3 double bond affects the specificity of product formation by CYP74 clan enzymes.…”

Section: Discussionmentioning

confidence: 99%

“…There are several distinct kinds of CYP74 enzymes, including two dehydrases, namely, allene oxide synthase (AOS) [ 18 ] and divinyl ether synthase (DES) [ 19 ], and two isomerases, namely, hydroperoxide lyase (HPL, synonym hemiacetal synthase) [ 20 , 21 , 22 ] and epoxyalcohol synthase [ 15 , 17 , 23 , 24 , 25 ]. Moreover, some CYP74 enzymes possess dual HPL/EAS or trial HPL/EAS/AOS activities [ 26 , 27 , 28 , 29 ].…”

Section: Introductionmentioning

confidence: 99%

Detection of the First Epoxyalcohol Synthase/Allene Oxide Synthase (CYP74 Clan) in the Lancelet (Branchiostoma belcheri, Chordata)

Toporkova

Смирнова

Lantsova

et al. 2021

IJMS

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The CYP74 clan cytochromes (P450) are key enzymes of oxidative metabolism of polyunsaturated fatty acids in plants, some Proteobacteria, brown and green algae, and Metazoa. The CYP74 enzymes, including the allene oxide synthases (AOSs), hydroperoxide lyases, divinyl ether synthases, and epoxyalcohol synthases (EASs) transform the fatty acid hydroperoxides to bioactive oxylipins. A novel CYP74 clan enzyme CYP440A18 of the Asian (Belcher’s) lancelet (Branchiostoma belcheri, Chordata) was biochemically characterized in the present work. The recombinant CYP440A18 enzyme was active towards all substrates used: linoleate and α-linolenate 9- and 13-hydroperoxides, as well as with eicosatetraenoate and eicosapentaenoate 15-hydroperoxides. The enzyme specifically converted α-linolenate 13-hydroperoxide (13-HPOT) to the oxiranyl carbinol (9Z,11R,12R,13S,15Z)-11-hydroxy-12,13-epoxy-9,15-octadecadienoic acid (EAS product), α-ketol, 12-oxo-13-hydroxy-9,15-octadecadienoic acid (AOS product), and cis-12-oxo-10,15-phytodienoic acid (AOS product) at a ratio of around 35:5:1. Other hydroperoxides were converted by this enzyme to the analogous products. In contrast to other substrates, the 13-HPOT and 15-HPEPE yielded higher proportions of α-ketols, as well as the small amounts of cyclopentenones, cis-12-oxo-10,15-phytodienoic acid and its higher homologue, dihomo-cis-12-oxo-3,6,10,15-phytotetraenoic acid, respectively. Thus, the CYP440A18 enzyme exhibited dual EAS/AOS activity. The obtained results allowed us to ascribe a name “B. belcheri EAS/AOS” (BbEAS/AOS) to this enzyme. BbEAS/AOS is a first CYP74 clan enzyme of Chordata species possessing AOS activity.

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Iron and manganese lipoxygenases of plant pathogenic fungi and their role in biosynthesis of jasmonates

Oliw

2022

Archives of Biochemistry and Biophysics

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Epoxyalcohol synthase activity of the CYP74B enzymes of higher plants

Cited by 12 publications

References 45 publications

Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat Sturnira hondurensis

Detection of Unprecedented CYP74 Enzyme in Mammal: Hydroperoxide Lyase CYP74C44 of the Bat Sturnira hondurensis

Detection of the First Epoxyalcohol Synthase/Allene Oxide Synthase (CYP74 Clan) in the Lancelet (Branchiostoma belcheri, Chordata)

Iron and manganese lipoxygenases of plant pathogenic fungi and their role in biosynthesis of jasmonates

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