کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8301361 | 1537679 | 2018 | 38 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Double function hydroperoxide lyases/epoxyalcohol synthases (CYP74C) of higher plants: identification and conversion into allene oxide synthases by site-directed mutagenesis
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کلمات کلیدی
TICTMSOxylipins9-H(P)OD(9S,10E,12Z)-9-hydro(pero)xy-10,12-octadecadienoic acidtrimethylsilylHSQCEASIMACHPL13-H(P)OD(9Z,11E,13S)-13-hydro(pero)xy-9,11-octadecadienoic acidSite-directed mutagenesis - mutagenesis مواجه با سایتDES - ازAOS - بهtotal ion current - جریان یونی کلDivinyl ether synthase - دی دیینیل اتر سنتازEpoxyalcohol synthase - سنتاز اپوکسی الکلAllene oxide synthase - سنتاز اکسید آلنCytochrome P450 - سیتوکروم پی۴۵۰SIM - سیم کارتHeteronuclear single quantum coherence spectroscopy - طیف سنجی تک هسته ای تک هسته ای کوانتومیcorrelation spectroscopy - طیف سنجی همبستگیheteronuclear multiple-bond correlation spectroscopy - طیف سنجی همبستگی چند باند هترونیکی هسته ایMethyl - متیلselected ion monitoring - نظارت بر یون انتخاب شدهHMBC یا Heteronuclear Multiple Bond Correlation - همبستگی پیوند چندگانه ناجورهستهHydroperoxide lyase - هیدروپراکسید لیازCOSY - کثیفImmobilised metal affinity chromatography - کروماتوگرافی وابسته به فلز فلز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Double function hydroperoxide lyases/epoxyalcohol synthases (CYP74C) of higher plants: identification and conversion into allene oxide synthases by site-directed mutagenesis Double function hydroperoxide lyases/epoxyalcohol synthases (CYP74C) of higher plants: identification and conversion into allene oxide synthases by site-directed mutagenesis](/preview/png/8301361.png)
چکیده انگلیسی
The CYP74C subfamily of fatty acid hydroperoxide transforming enzymes includes hydroperoxide lyases (HPLs) and allene oxide synthases (AOSs). This work reports a new facet of the putative CYP74C HPLs. Initially, we found that the recombinant CYP74C13_MT (Medicago truncatula) behaved predominantly as the epoxyalcohol synthase (EAS) towards the 9(S)-hydroperoxide of linoleic acid. At the same time, the CYP74C13_MT mostly possessed the HPL activity towards the 13(S)-hydroperoxides of linoleic and α-linolenic acids. To verify whether this dualistic behaviour of CYP74C13_MT is occasional or typical, we also examined five similar putative HPLs (CYP74C). These were CYP74C4_ST (Solanum tuberosum), CYP74C2 (Cucumis melo), CYP74C1_CS and CYP74C31 (both of Cucumis sativus), and CYP74C13_GM (Glycine max). All tested enzymes behaved predominantly as EAS toward 9-hydroperoxide of linoleic acid. Oxiranyl carbinols such as (9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acids were the major EAS products. Besides, the CYP74C31 possessed an additional minor 9-AOS activity. The mutant forms of CYP74C13_MT, CYP74C1_CS, and CYP74C31 with substitutions at the catalytically essential domains, namely the “hydroperoxide-binding domain” (I-helix), or the SRS-1 domain near the N-terminus, showed strong AOS activity. These HPLs to AOSs conversions were observed for the first time. Until now a large part of CYP74C enzymes has been considered as 9/13-HPLs. Notwithstanding, these results show that all studied putative CYP74C HPLs are in fact the versatile HPL/EASs that can be effortlessly mutated into specific AOSs.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1863, Issue 4, April 2018, Pages 369-378
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1863, Issue 4, April 2018, Pages 369-378
نویسندگان
Yana Y. Toporkova, Svetlana S. Gorina, Elena K. Bessolitsyna, Elena O. Smirnova, Valeria S. Fatykhova, Fredi Brühlmann, Tatiana M. Ilyina, Lucia S. Mukhtarova, Alexander N. Grechkin,