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Literature summary extracted from

  • Pan, X.; Chen, G.; Kazachkov, M.; Greer, M.S.; Caldo, K.M.; Zou, J.; Weselake, R.J.
    In vivo and in vitro evidence for biochemical coupling of reactions catalyzed by lysophosphatidylcholine acyltransferase and diacylglycerol acyltransferase (2015), J. Biol. Chem., 290, 18068-18078.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.20 expressed in Saccharomyces cerevisiae mutant H1246 Linum usitatissimum
2.3.1.23 two genes LPCAT, LPCAT1 and LPCAT2, containing eight exons and seven introns, respectively, DNA and amino acid seqquence determination and analysis, co-expression of flax genes LPCAT1 and diacylglycerol acyltransferase DGAT1-1 in the yeast quintuple mutant strain H1246 DELTAale1 significantly increasing 18-carbon polyunsaturated fatty acids in triacylglycerol with a concomitant decrease of 18-carbon polyunsaturated fatty acids in phospholipid. The specific activity of flax LPCAT1-catalyzed forward reaction is about 1000 times higher than that of flax DGAT1-catalyzed reaction when the expressed recombinant enzymes are assessed in yeast microsomes under in vitro enzyme assays Linum usitatissimum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.23 microsome
-
Linum usitatissimum
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.23 acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine Linum usitatissimum phosphatidylcholine is the major site for polyunsaturated fatty acid synthesis CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.20 Linum usitatissimum
-
-
-
2.3.1.23 Linum usitatissimum
-
isozymes LPCAT1 and LPCAT2
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.20 additional information co-expressing flax diacylglycerol acyltransferase1-1 (DGAT1-1) and acyl-CoA:lysophosphatidylcholine acyltransferase1 (LPCAT1) in a yeast quintuple mutant significantly increases 18-carbon polyunsaturated fatty acids in triacylglycerol with a concomitant decrease of 18-carbon polyunsaturated fatty acids in phospholipid. The specific activity of overall LPCAT1 and DGAT1-1 coupling process exhibited a preference for transferring 14C-labeled linoleoyl or linolenoyl than oleoyl moieties from the sn-2 position of phosphatidylcholine to triacylglycerol Linum usitatissimum ?
-
?
2.3.1.20 oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
-
Linum usitatissimum CoA + trioleoylglycerol
-
?
2.3.1.23 acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine phosphatidylcholine is the major site for polyunsaturated fatty acid synthesis Linum usitatissimum CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
r
2.3.1.23 acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine the reverse reaction of enzyme LPCAT uses phosphatidylcholine as substrate and forms acyl-CoA and lysophosphatidylcholine Linum usitatissimum CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
r

Synonyms

EC Number Synonyms Comment Organism
2.3.1.20 DGAT
-
Linum usitatissimum
2.3.1.20 diacylglycerol acyltransferase
-
Linum usitatissimum
2.3.1.23 acyl-CoA:lysophosphatidylcholine acyltransferase
-
Linum usitatissimum
2.3.1.23 LPCAT
-
Linum usitatissimum
2.3.1.23 LPCAT1
-
Linum usitatissimum
2.3.1.23 LPCAT2
-
Linum usitatissimum
2.3.1.23 lysophosphatidylcholine acyltransferase
-
Linum usitatissimum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.23 30
-
assay at, forward and reverse reaction Linum usitatissimum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.23 7.2
-
assay at, forward and reverse reaction Linum usitatissimum

General Information

EC Number General Information Comment Organism
2.3.1.23 evolution the LPCAT genes are highly conserved, suggesting that the duplicated LPCAT genes were derived from a segmental duplication event. The segmental duplication is the result of a recent whole-genome duplication event in flax Linum usitatissimum
2.3.1.23 metabolism the enzyme is involved in the Kennedy pathway for triacylglycerol synthesis, biochemical coupling of isozyme LPCAT1 and the diacylglycerol acyltransferase DGAT1-1-catalyzed reactions, overview. Both enzymes are required for synthesis of triacylgycerol Linum usitatissimum
2.3.1.23 additional information the specific activity of flax LPCAT1-catalyzed forward reaction is about 1000 times higher than that of flax DGAT1-catalyzed reaction when the coexpressed recombinant enzymes are assessed in yeast microsomes under in vitro enzyme assays, overview Linum usitatissimum
2.3.1.23 physiological function phosphatidylcholine is the major site for polyunsaturated fatty acid synthesis. Enzyme lysophosphatidylcholine acyltransferase can transfer polyunsaturated fatty acids on phosphatidylcholine directly into the acyl-CoA pool, making these polyunsaturated fatty acids available for the diacylglycerol acyltransferase (DGAT)-catalyzed reaction for triacylglycerol production, proposed mechanism, overview Linum usitatissimum