Acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) of Camelina sativa seeds: biochemical properties and function
Sylwia Klińska , Katarzyna Jasieniecka-Gazarkiewicz , Antoni Banaś
AbstractThe transfer of polyunsaturated fatty acids from the location of their synthesis (phosphatidylcholine) to other lipids, e.g., triacylglycerol, remains insufficiently understood. Several enzymes could be involved in this process. One of these enzymes is acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs). In Camelina sativa seeds, LPCATs could be one of the most important players in this process. Our data clearly indicate that the CsLPCATs present in developing seeds have the potential to transfer almost all polyunsaturated fatty acids synthesised on phosphatidylcholine to the acyl-CoA pool. CsLPCAT activity is the highest at 30 °C, and the enzymes operate well at a pH of 7.0–11.0, with the best activity at a pH of 9.0. The activity of CsLPCATs was inhibited by calcium and magnesium ions at a concentration of 0.05–2 mM. In the forward reaction, CsLPCATs preferentially utilise 18:2-CoA; however, other C18 unsaturated fatty acids are also well accepted. In the backward reactions, there is no clear discrimination between the C18 unsaturated fatty acids utilised by the enzymes for phosphatidylcholine remodelling. The activity of CsLPCATs does not differ much between the stages of seed development.
|Journal series||Planta, ISSN 0032-0935, e-ISSN 1432-2048, (N/A 100 pkt)|
|Publication size in sheets||0.75|
|Keywords in English||False flax, acyl-CoA, lysophosphatidylcholine acyltransferases, phosphatidylcholine remodelling, seed lipids, TAG biosynthesis, triacylglycerol|
|License||Other; published final; ; with publication|
|Score||= 100.0, 28-01-2020, ArticleFromJournal|
|Publication indicators||: 2017 = 1.203; : 2018 = 3.06 (2) - 2018=3.408 (5)|
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