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Literature summary extracted from

  • 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 (2016), Lipids, 51, 15-23 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.23 gene AtLPCAT2, recombinant overexpression in Saccharomyces cerevisiae haploid ALE1-knockout strain (BY4742, Matalpa, his3DELTA1, leu2DELTA0, lys2DELTA0, ura3DELTA0, YOR175c::kanMX4) Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.23 additional information recombinant expression of Arabidopsis thaliana LPCAT2, differences in incorporation of [14C]oleoyl-CoA into PtdCho in microsomal preparations of ale1 yeast expressing AtLPCAT2 with and without DTNB, overview Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.23 DTNB complete inhibition of LPCAT in wild-type and in recombinant heterologous yeast microsomes Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.23 microsome
-
 Saccharomyces cerevisiae
-
-
2.3.1.23 microsome
-
 Arabidopsis thaliana
-
-
2.3.1.51 microsome
-
 Saccharomyces cerevisiae
-
-
2.3.1.121 microsome
-
 Arabidopsis thaliana
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.23 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid Arabidopsis thaliana
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine Saccharomyces cerevisiae
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine Arabidopsis thaliana
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine Saccharomyces cerevisiae
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine Arabidopsis thaliana
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.51 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid Saccharomyces cerevisiae
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.51 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine Saccharomyces cerevisiae
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.121 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid Arabidopsis thaliana
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.121 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine Arabidopsis thaliana
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 r
2.3.1.121 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine Arabidopsis thaliana
-
 CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.23 Arabidopsis thaliana Q9CAN8
-
-
2.3.1.23 Saccharomyces cerevisiae Q08548
-
-
2.3.1.51 Saccharomyces cerevisiae P33333
-
-
2.3.1.121 Arabidopsis thaliana Q8S8S2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.23 additional information substrate specificity (towards different acyl acceptors) of the lysophospholipid:acyl-CoA acyltransferase in the forward reactions with [14C]oleoyl-CoA, assay optimization. Lysophosphatidylcholine is by far the best substrate for AtLPCAT2. Ratio between reverse and forward activities for different LPLATs for different phospholipids, overview. Highest amounts in PtdCho with AtLPCAT2 Arabidopsis thaliana ?
-
-
2.3.1.23 additional information substrate specificity (towards different acyl acceptors) of the lysophospholipid:acyl-CoA acyltransferase in the forward reactions with [14C]oleoyl-CoA, assay optimization. Ratio between reverse and forward activities for different LPLATs for different phospholipids, overview. Very high activity in the forward reaction by the Ale1, while its ability to operate reversibly on all tested lipids is very low, highest amounts in PtdCho Saccharomyces cerevisiae ?
-
-
2.3.1.23 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid
-
 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid low activity, cf. EC 2.3.1.51 Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid very low activity, cf. EC 2.3.1.51 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine
-
 Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine
-
 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine preferred substrate, high activity Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine preferred substrate, high activity Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
-
 Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
-
 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine low activity, cf. EC 2.3.1.121 Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.23 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine very low activity, cf. EC 2.3.1.121 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.51 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 Saccharomyces cerevisiae ?
-
-
2.3.1.51 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid
-
 Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.51 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid preferred substrate. Slc1 has a very high capacity of reversibility towards the PtdOH substrate Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.51 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine low activity, cf. EC 2.3.1.23. Slc1 has no detectable reverse reaction towards PtdCho substrate Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 ir
2.3.1.51 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
-
 Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.51 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine lower activity, cf. EC 2.3.1.121 Saccharomyces cerevisiae CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.121 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. AtLPEAT2 incorporated similar amounts in PtdCho and PtdEtn by exchange Arabidopsis thaliana ?
-
-
2.3.1.121 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid
-
 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.121 oleoyl-CoA + 1-oleoyl-lysophosphatidic acid cf. EC 2.3.1.51 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
-
 r
2.3.1.121 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine
-
 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 r
2.3.1.121 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine cf. EC 2.3.1.23 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
-
 r
2.3.1.121 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
-
 Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r
2.3.1.121 oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine preferred substrate Arabidopsis thaliana CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.3.1.23 ALE1
-
 Saccharomyces cerevisiae
2.3.1.23 AtLPLAT2
-
 Arabidopsis thaliana
2.3.1.23 LPCAT2
-
 Arabidopsis thaliana
2.3.1.23 LPLAT
-
 Saccharomyces cerevisiae
2.3.1.23 LPLAT
-
 Arabidopsis thaliana
2.3.1.23 lysophospholipid acyltransferase
-
 Saccharomyces cerevisiae
2.3.1.23 lysophospholipid acyltransferase
-
 Arabidopsis thaliana
2.3.1.23 lysophospholipid:acyl-CoA acyltransferase
-
 Saccharomyces cerevisiae
2.3.1.23 lysophospholipid:acyl-CoA acyltransferase
-
 Arabidopsis thaliana
2.3.1.23 More see also EC 2.3.1.121 and EC 2.3.1.51 Saccharomyces cerevisiae
2.3.1.23 More see also EC 2.3.1.121 and EC 2.3.1.51 Arabidopsis thaliana
2.3.1.51 LPAAT
-
 Saccharomyces cerevisiae
2.3.1.51 lysophosphatidic acid acyltransferase
-
 Saccharomyces cerevisiae
2.3.1.51 lysophospholipid:acyl-CoA acyltransferase
-
 Saccharomyces cerevisiae
2.3.1.51 More cf. EC 2.3.1.121 and EC 2.3.1.23 Saccharomyces cerevisiae
2.3.1.51 Scl1
-
 Saccharomyces cerevisiae
2.3.1.121 LPEAT2
-
 Arabidopsis thaliana
2.3.1.121 LPLAT
-
 Arabidopsis thaliana
2.3.1.121 lysophospholipid acyltransferase
-
 Arabidopsis thaliana
2.3.1.121 lysophospholipid:acyl-CoA acyltransferase
-
 Arabidopsis thaliana
2.3.1.121 More see also EC 2.3.1.23 and EC 2.3.1.51 Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.23 30
-
 assay at Saccharomyces cerevisiae
2.3.1.23 30
-
 assay at Arabidopsis thaliana
2.3.1.51 30
-
 assay at Saccharomyces cerevisiae
2.3.1.121 30
-
 assay at Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.23 7.2
-
 assay at Saccharomyces cerevisiae
2.3.1.23 7.2
-
 assay at Arabidopsis thaliana
2.3.1.51 7.2
-
 assay at Saccharomyces cerevisiae
2.3.1.121 7.2
-
 assay at Arabidopsis thaliana