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Editing of phosphatidic acid and phosphatidylethanolamine by acyl-CoA: lysophospholipid acyltransferases in developing Camelina sativa seeds
Main conclusions The main source of polyunsaturated acyl-CoA in cytoplasmic acyl-CoA pool of Camelina sativa seeds are fatty acids derived from phosphatidylcholine followed by phosphatidic acid. Contribution of phosphatidylethanolamine is negligible. While phosphatidylethanolamine (PE) is the second...
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Published in: | Planta 2020-07, Vol.252 (1), p.4-4, Article 4 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Main conclusions
The main source of polyunsaturated acyl-CoA in cytoplasmic acyl-CoA pool of Camelina sativa seeds are fatty acids derived from phosphatidylcholine followed by phosphatidic acid. Contribution of phosphatidylethanolamine is negligible.
While phosphatidylethanolamine (PE) is the second most abundant phospholipid, phosphatidic acid (PA) only constitutes a small fraction of
C. sativa
seeds’ polar lipids. In spite of this, the relative contribution of PA in providing fatty acids for the synthesis of acyl-CoA, supplying cytosolic acyl-CoA pool seems to be much higher than the contribution of PE. Our data indicate that up to 5% of fatty acids present in mature
C. sativa
seeds are first esterified with PA, in comparison to 2% first esterified with PE, before being transferred into acyl-CoA pool via backward reactions of either acyl-CoA:lysophosphatidic acid acyltransferases (
Cs
LPAATs) or acyl-CoA:lysophoshatidylethanolamine acyltransferases (
Cs
LPEATs). Those acyl-CoAs are later reused for lipid biosynthesis or remodelling. In the forward reactions both aforementioned acyltransferases display the highest activity at 30 °C. The spectrum of optimal pH differs for both enzymes with
Cs
LPAATs most active between pH 7.5–9.0 and
Cs
LPEATs between pH 9.0 to 10.0. Whereas addition of magnesium ions stimulates
Cs
LPAATs, calcium and potassium ions inhibit them in concentrations of 0.05–2.0 mM. All three types of ions inhibit
Cs
LPEATs activity. Both tested acyltransferases present the highest preferences towards 16:0-CoA and unsaturated 18-carbon acyl-CoAs in forward reactions. However,
Cs
LPAATs preferentially utilise 18:1-CoA and
Cs
LPEATs preferentially utilise 18:2-CoA while catalysing fatty acid remodelling of PA and PE, respectively. |
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ISSN: | 0032-0935 1432-2048 |
DOI: | 10.1007/s00425-020-03408-z |