title: Possible Role of Different Yeast and Plant Lysophospholipid:Acyl-CoA Acyltransferases (LPLATs) in Acyl Remodelling of Phospholipids.
abstract: Recent results have suggested that plant lysophosphatidylcholine:acyl-coenzyme A acyltransferases (LPCATs) can operate in reverse in vivo and thereby catalyse an acyl exchange between the acyl-coenzyme A (CoA) pool and the phosphatidylcholine. We have investigated the abilities of Arabidopsis AtLPCAT2, Arabidopsis lysophosphatidylethanolamine acyltransferase (LPEAT2), S. cerevisiae lysophospholipid acyltransferase (Ale1) and S. cerevisiae lysophosphatidic acid acyltransferase (SLC1) to acylate lysoPtdCho, lysoPtdEtn and lysoPtdOH and act reversibly on the products of the acylation; the PtdCho, PtdEtn and PtdOH. The tested LPLATs were expressed in an S. cervisiae ale1 strain and enzyme activities were assessed in assays using microsomal preparations of the different transformants. The results show that, despite high activity towards lysoPtdCho, lysoPtdEtn and lysoPtdOH by the ALE1, its capacities to operate reversibly on the products of the acylation were very low. Slc1 readily acylated lysoPtdOH, lysoPtdCho and lysoPtdEtn but showed no reversibility towards PtdCho, very little reversibility towards PtdEtn and very high reversibility towards PtdOH. LPEAT2 showed the highest levels of reversibility towards PtdCho and PtdEtn of all LPLATs tested but low ability to operate reversibly on PtdOH. AtLPCAT2 showed good reversible activity towards PtdCho and PtdEtn and very low reversibility towards PtdOH. Thus, it appears that some of the LPLATs have developed properties that, to a much higher degree than other LPLATs, promote the reverse reaction during the same assay conditions and with the same phospholipid. The results also show that the capacity of reversibility can be specific for a particular phospholipid, albeit the lysophospholipid derivatives of other phospholipids serve as good acyl acceptors for the forward reaction of the enzyme.
authors.affiliation: Intercollegiate Faculty of Biotechnology, University of Gdańsk and Medical University of Gdańsk, Kładki 24, 80-822, Gdańsk, Poland.
authors.forename: Katarzyna
authors.initials: K
authors.lastname: Jasieniecka-Gazarkiewicz
authors.affiliation: Intercollegiate Faculty of Biotechnology, University of Gdańsk and Medical University of Gdańsk, Kładki 24, 80-822, Gdańsk, Poland.
authors.forename: Kamil
authors.initials: K
authors.lastname: Demski
authors.affiliation: Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden.
authors.forename: Ida
authors.initials: I
authors.lastname: Lager
authors.affiliation: Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden.
authors.forename: Sten
authors.initials: S
authors.lastname: Stymne
authors.affiliation: Intercollegiate Faculty of Biotechnology, University of Gdańsk and Medical University of Gdańsk, Kładki 24, 80-822, Gdańsk, Poland. banas@biotech.ug.gda.pl.
authors.forename: Antoni
authors.initials: A
authors.lastname: Banaś
mesh_terms: D000102:Acetyl-CoA C-Acyltransferase / Q000378:metabolism*; D000215:Acylation; D017360:Arabidopsis / Q000201:enzymology* / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000378:metabolism*
chemical_list: D010743:Phospholipids; D000102:Acetyl-CoA C-Acyltransferase
keywords: Ale1; LPCAT; LPEAT; Microsomal preparation; Phospholipids; Slc1