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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Slc1p and Slc4p both active as acyltransferases, involved in fatty acid exchange of mature glycerophospholipids
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
-
-
-
?
acyl-CoA + 2-acyl-sn-glycerol 3-phosphate
CoA + ?
-
the rate of CoA-liberation is much lower than with 1-acyl-sn-glycerol 3-phosphate
-
?
oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
oleoyl-CoA + 1-oleoyl-sn-glycerol-3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
substrate preference higher for oleoyl-CoA than for palmitoyl-CoA and stearoyl-CoA
-
-
?
oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine
CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
low activity, cf. EC 2.3.1.23. Slc1 has no detectable reverse reaction towards PtdCho substrate
-
-
ir
oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
oleoyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
additional information
?
-
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
i.e. lysophosphatidic acid, highly specific for 1-acyl-sn-glycerol 3-phosphate, catalyzes acylation of position 2 hydroxyl-group
i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
effect of substrate concentration
i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme utilizes saturated and unsaturated acyl-CoAs at comparable rates
i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
acyltranferase activity by Slc1p and Slc4p
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
glycerophospholipid profile similar between Slc1p and Slc4p
-
-
?
oleoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
-
-
r
oleoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
preferred substrate. Slc1 has a very high capacity of reversibility towards the PtdOH substrate
-
-
r
oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
-
-
r
oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
lower activity, cf. EC 2.3.1.121
-
-
r
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
substrate preference lower than for oleoyl-CoA
-
-
?
additional information
?
-
-
very broad specificity for acyl-CoAs, the enzyme does not seem to discriminate strictly the cis and trans configurations or the position of double bond in the fatty acyl moiety
-
-
?
additional information
?
-
no substrates: lysophosphatidyl choline, lysophosphatidyl ethanolamine, lysophosphatidyl glycerol, and lysophosphatidyl inositol
-
-
?
additional information
?
-
-
no substrates: lysophosphatidyl choline, lysophosphatidyl ethanolamine, lysophosphatidyl glycerol, and lysophosphatidyl inositol
-
-
?
additional information
?
-
comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and tiacylglycerols, overview. The yeast LPAAT Slc1p or ScLPAAT has been shown to have activity with 22:1-CoA in addition to 18:1-CoA substrates, indicating a broad substrate specificity with respect to chain length although 22:6-CoA, 22:5-CoA, and other LC-PUFAs has not been tested as substrates
-
-
-
additional information
?
-
substrate specificity (towards different acyl acceptors) of the lysophospholipid:acyl-CoA acyltransferase in the forward reactions with [14C]18:1-CoA, assay optimization. Ratio between reverse and forward activities for different LPLATs for different phospholipids, overview
-
-
-
additional information
?
-
-
substrate specificity (towards different acyl acceptors) of the lysophospholipid:acyl-CoA acyltransferase in the forward reactions with [14C]18:1-CoA, assay optimization. Ratio between reverse and forward activities for different LPLATs for different phospholipids, overview
-
-
-
additional information
?
-
the enzyme shows a preference for acylating long-chain fatty acids. Substrate specificity is evaluated with 18:1- or 22:6-LPA, and 18:3-, 20:5-, 22:5-, 22:6-CoAs. Mortierella alpina LPAAT has the highest substrate specificity for accumulating DHA onto oleoyl-lysophosphatidic acid (oleoyl-LPA), while the plant LPAATs tested show lower preference for docosahexaenoic acid (DHA). Competition among acyl donor substrates for LPAATs, overview
-
-
-
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Slc1p and Slc4p both active as acyltransferases, involved in fatty acid exchange of mature glycerophospholipids
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
-
-
-
?
oleoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
-
-
r
oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
-
-
r
additional information
?
-
comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and tiacylglycerols, overview. The yeast LPAAT Slc1p or ScLPAAT has been shown to have activity with 22:1-CoA in addition to 18:1-CoA substrates, indicating a broad substrate specificity with respect to chain length although 22:6-CoA, 22:5-CoA, and other LC-PUFAs has not been tested as substrates
-
-
-
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
acyltranferase activity by Slc1p and Slc4p
-
-
?
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additional information
microsomal enzyme activity not completely lost by deletion of Slc1p, evidence for additional enzyme activity, SLC4 gene encodes second enzmye indicated by lethality of double mutants of Slc1p and Slc4p, same glycerophospholipid profile but different lipid profiles between Slc1p and Slc4p, different substrate specificity between Slc1p and Slc4p or access to different lysoglycerophospholipid substrates because of a different subcellular location
additional information
microsomal enzyme activity not completely lost by deletion of Slc1p, evidence for additional enzyme activity, SLC4 gene encodes second enzmye indicated by lethality of double mutants of Slc1p and Slc4p, same glycerophospholipid profile but different lipid profiles between Slc1p and Slc4p, different substrate specificity between Slc1p and Slc4p or access to different lysoglycerophospholipid substrates because of a different subcellular location
additional information
-
microsomal enzyme activity not completely lost by deletion of Slc1p, evidence for additional enzyme activity, SLC4 gene encodes second enzmye indicated by lethality of double mutants of Slc1p and Slc4p, same glycerophospholipid profile but different lipid profiles between Slc1p and Slc4p, different substrate specificity between Slc1p and Slc4p or access to different lysoglycerophospholipid substrates because of a different subcellular location
additional information
-
absence of transmembrane domains, presence of hydrolase/acyltransferase domain with a distinct lipid-binding motif and a lysophospholipase domain, reduced phosphatidic acid in mutants suggests a role in phosphatidic acid biosynthesis, overexpression shows increase in phosphatidic acid and other phospholipids on organic solvent exposure, recombinant protein acylates lysophosphatidic acid, substrate preference analyzed, nearly no activity with lysophospholipids such as lysophosphatidylcholine (LPC), lysophosphatidylethanolamine (LPE), and lysophosphatidylserine (LPS)
additional information
deletion of Slc1p alone not lethal, microsomal enzyme activity not completely lost, evidence for additional enzyme activity, comparison between Slc1p with Slc4p, single mutants of Slc1p and Slc4p generated, double mutant of Slc1p and Slc4p lethal, same glycerophospholipid profiles but different lipid profiles between Slc1p and Slc4p, both enzymes able to use endogenous lysoglycerophospholipids as substrates, substrate specificity between Slc1p and Slc4p different or access to different lysoglycerophospholipid substrates because of a different subcellular location, Slc1p and Slc4p are both active as acyltransferases and are also involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids
additional information
deletion of Slc1p alone not lethal, microsomal enzyme activity not completely lost, evidence for additional enzyme activity, comparison between Slc1p with Slc4p, single mutants of Slc1p and Slc4p generated, double mutant of Slc1p and Slc4p lethal, same glycerophospholipid profiles but different lipid profiles between Slc1p and Slc4p, both enzymes able to use endogenous lysoglycerophospholipids as substrates, substrate specificity between Slc1p and Slc4p different or access to different lysoglycerophospholipid substrates because of a different subcellular location, Slc1p and Slc4p are both active as acyltransferases and are also involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids
additional information
-
deletion of Slc1p alone not lethal, microsomal enzyme activity not completely lost, evidence for additional enzyme activity, comparison between Slc1p with Slc4p, single mutants of Slc1p and Slc4p generated, double mutant of Slc1p and Slc4p lethal, same glycerophospholipid profiles but different lipid profiles between Slc1p and Slc4p, both enzymes able to use endogenous lysoglycerophospholipids as substrates, substrate specificity between Slc1p and Slc4p different or access to different lysoglycerophospholipid substrates because of a different subcellular location, Slc1p and Slc4p are both active as acyltransferases and are also involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids
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Yamada, K.; Okuyama, H.; Endo, Y.; Ikezawa, H.
Acyltransferase systems involved in phospholipid metabolism in Saccharomyces cerevisiae
Arch. Biochem. Biophys.
183
281-289
1977
Saccharomyces cerevisiae, Saccharomyces cerevisiae OC-2
brenda
Benghezal, M.; Roubaty, C.; Veepuri, V.; Knudsen, J.; Conzelmann, A.
SLC1 and SLC4 encode partially redundant acyl-coenzyme A 1-acylglycerol-3-phosphate O-acyltransferases of budding yeast
J. Biol. Chem.
282
30845-30855
2007
Saccharomyces cerevisiae (P33333), Saccharomyces cerevisiae (Q08548), Saccharomyces cerevisiae
brenda
Ghosh, A.K.; Ramakrishnan, G.; Rajasekharan, R.
YLR099C (ICT1) encodes a soluble Acyl-CoA-dependent lysophosphatidic acid acyltransferase responsible for enhanced phospholipid synthesis on organic solvent stress in Saccharomyces cerevisiae
J. Biol. Chem.
283
9768-9775
2008
Saccharomyces cerevisiae
brenda
Pagac, M.; de la Mora, H.V.; Duperrex, C.; Roubaty, C.; Vionnet, C.; Conzelmann, A.
Topology of 1-acyl-sn-glycerol-3-phosphate acyltransferases SLC1 and ALE1 and related membrane-bound O-acyltransferases (MBOATs) of Saccharomyces cerevisiae
J. Biol. Chem.
286
36438-36447
2011
Saccharomyces cerevisiae (P33333), Saccharomyces cerevisiae (Q08548), Saccharomyces cerevisiae
brenda
Ayciriex, S.; Le Guedard, M.; Camougrand, N.; Velours, G.; Schoene, M.; Leone, S.; Wattelet-Boyer, V.; Dupuy, J.W.; Shevchenko, A.; Schmitter, J.M.; Lessire, R.; Bessoule, J.J.; Testet, E.
YPR139c/LOA1 encodes a novel lysophosphatidic acid acyltransferase associated with lipid droplets and involved in TAG homeostasis
Mol. Biol. Cell
23
233-246
2012
Saccharomyces cerevisiae (Q06508), Saccharomyces cerevisiae
brenda
Shrestha, P.; Hussain, D.; Mulder, R.J.; Taylor, M.C.; Singh, S.P.; Petrie, J.R.; Zhou, X.R.
Increased DHA production in seed oil using a selective lysophosphatidic acid acyltransferase
Front. Plant Sci.
9
1234
2018
Mortierella alpina, Yarrowia lipolytica (A0A1D8NJ27), Micromonas pusilla (C1MQM1), Saccharomyces cerevisiae (P33333), Limnanthes alba (Q42868), Arabidopsis thaliana (Q8LG50), Brassica napus (Q9LLY4), Emiliania huxleyi (R1BZP3), Emiliania huxleyi
brenda
Jasieniecka-Gazarkiewicz, K.; Demski, K.; Lager, I.; Stymne, S.; Banas, A.
Possible role of different yeast and plant lysophospholipid acyl-CoA acyltransferases (LPLATs) in acyl remodelling of phospholipids
Lipids
51
15-23
2016
Saccharomyces cerevisiae (P33333), Saccharomyces cerevisiae
brenda