دورية أكاديمية
Camelina sativa phosphatidylcholine:diacylglycerol cholinephosphotransferase-catalyzed interconversion does not discriminate between substrates.
| العنوان: | Camelina sativa phosphatidylcholine:diacylglycerol cholinephosphotransferase-catalyzed interconversion does not discriminate between substrates. |
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| المؤلفون: | Demski K; Department of Plant Breeding, Swedish University of Agriculture Science, Alnarp, Sweden., Jeppson S; Department of Plant Breeding, Swedish University of Agriculture Science, Alnarp, Sweden., Stymne S; Department of Plant Breeding, Swedish University of Agriculture Science, Alnarp, Sweden., Lager I; Department of Plant Breeding, Swedish University of Agriculture Science, Alnarp, Sweden. |
| المصدر: | Lipids [Lipids] 2021 Nov; Vol. 56 (6), pp. 591-602. Date of Electronic Publication: 2021 Aug 31. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Wiley Subscription Services, Inc Country of Publication: United States NLM ID: 0060450 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1558-9307 (Electronic) Linking ISSN: 00244201 NLM ISO Abbreviation: Lipids Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2018- : Hoboken, NJ : Wiley Subscription Services, Inc. Original Publication: Chicago, American Oil Chemists' Society. |
| مواضيع طبية MeSH: | Brassicaceae* , Diacylglycerol Cholinephosphotransferase*, Catalysis ; Fatty Acids ; Phosphatidylcholines ; Seeds ; Triglycerides |
| مستخلص: | Phosphatidylcholine:diacylglycerol cholinephosphotransferases (PDCT) regulate the fatty acid composition of seed oil (triacylglycerol, TAG) by interconversion of diacylglycerols (DAG) and phosphatidylcholine (PtdCho). PtdCho is the substrate for polyunsaturated fatty acid biosynthesis, as well as for a number of unusual fatty acids. By the action of PDCT, these fatty acids can be transferred into the DAG pool to be utilized in TAG biosynthesis by the action of acyl-CoA:DAG and phospholipid:diacylglycerol acyltransferases. Despite its importance in regulating seed oil composition, biochemical characterization of PDCT enzymes has been lacking. We characterized Camelina sativa PDCT in microsomal preparations of a yeast strain expressing Camelina PDCT and lacking the capacity of producing TAG. Camelina PDCT was specific for PtdCho and the sn-1,2 enantiomer of DAG and could not utilize ceramide. The interconversion reaches equilibrium within 15 min of incubation, indicating that only distinct pools of DAG and PtdCho were available for exchange. However, the pool sizes of DAG and PtdCho involved in the exchange were not fixed but increased with the amount of exogenous DAG or PtdCho added. Camelina PDCT showed about the same selectivity for di-oleoyl, di-linoleoyl, and di-linolenoyl species in both PtdCho and DAG substrates, suggesting that no unidirectional transfer of particular unsaturated substrates occurred. Camelina PDCT had a good activity with erucoyl-DAG as a substrate despite low erucic acid levels in PtdCho in plant species accumulating a high amount of this fatty acid in the seed oil. (© 2021 The Authors. Lipids published by Wiley Periodicals LLC on behalf of AOCS.) |
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| فهرسة مساهمة: | Keywords: Camelina; PDCT; acyltransferase; diacylglycerol; phosphatidylcholine; seed oil |
| المشرفين على المادة: | 0 (Fatty Acids) 0 (Phosphatidylcholines) 0 (Triglycerides) EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase) |
| تواريخ الأحداث: | Date Created: 20210831 Date Completed: 20220127 Latest Revision: 20220127 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1002/lipd.12322 |
| PMID: | 34463366 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1558-9307 |
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| DOI: | 10.1002/lipd.12322 |