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(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + palmitoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-sn-glycerol 3-phosphate
Substrates: highest activity
Products: -
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(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-CoA + 1-stearoyl-sn-glycerol 3-phosphate
CoA + 1-stearoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-lysophosphatidic acid
Substrates: -
Products: -
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1-oleoyl-sn-glycerol-3-phosphate + oleoyl-CoA
CoA + 1,2-oleoyl-sn-glycerol-3-phosphate
-
Substrates: -
Products: -
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1-oleoyl-sn-glycerol-3-phosphate + palmitoyl-CoA
CoA + 1-oleoyl-2-palmitoyl-sn-glycerol-3-phosphate
-
Substrates: -
Products: -
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acyl-ACP + 1-acyl-sn-glycerol 3-phosphate
ACP + 1,2-diacyl-sn-glycerol 3-phosphate
acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
acyl-CoA + 1-arachidonoyl-sn-glycerol 3-phosphate
CoA + 1-arachidonoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: less efficient than 1-acyl-sn-glycerol 3-phosphate
Products: -
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acyl-CoA + 1-lauroyl-sn-glycerol 3-phosphate
CoA + 1-lauroyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: assayed using coconut cDNA encoding a 299-amino acid protein with enzyme activity expressed in canola seeds
Products: -
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acyl-CoA + 1-O-alkyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: the activity is approximately half of that toward 1-acyl-sn-glycerol 3-phosphate
Products: -
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acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
acyl-CoA + 1-oleoyl-lysophosphatidylethanolamine
CoA + 1-oleoyl-2-acyl-lysophosphatidylethanolamine
acyl-CoA + 1-oleoyl-lysophosphatidylglycerol
CoA + 1-oleoyl-2-acyl-lysophosphatidylglycerol
Substrates: low activity
Products: -
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acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-acyl-sn-glycerol 3-phosphate
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
acyl-CoA + 1-palmitoleoyl-lysophosphatidic acid
CoA + 1-palmitoleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
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acyl-CoA + 1-palmitoyl-lysophosphatidic acid
CoA + 1-palmitoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
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acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
acyl-CoA + 1-stearoyl-sn-glycerol 3-phosphate
CoA + 1-stearoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: less efficient than 1-acyl-sn-glycerol 3-phosphate
Products: -
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acyl-CoA + 2-acyl-sn-glycerol 3-phosphate
CoA + ?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
acyl-[acyl-carrier protein] + 1-acyl-sn-glycerol 3-phosphate
ACP + 1,2-diacyl-sn-glycerol 3-phosphate
acyl-[acyl-carrier protein] + 1-acyl-sn-glycerol 3-phosphate
acyl-carrier protein + 1,2-diacyl-sn-glycerol 3-phosphate
alpha-linolenoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-alpha-linolenoyl-lysophosphatidic acid
Substrates: -
Products: -
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arachidonoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-arachidonoyl-lysophosphatidic acid
Substrates: -
Products: -
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arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
arachidonoyl-CoA + 1-arachidonoyl-2-lyso-sn-phosphatidylcholine
CoA + 1,2-diarachidonoyl-sn-phosphatidylcholine
Substrates: -
Products: -
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arachidonoyl-CoA + 1-arachidonoyl-sn-glycerol 3-phosphate
CoA + 1,2-diarachidonoyl-sn-glycerol 3-phosphate
Substrates: slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
Products: -
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arachidonoyl-CoA + 1-octadecenyl-2-lysophosphatidylinositol
CoA + 1-octadecenyl-2-arachidonoylphosphatidylinositol
C4B4E7
Substrates: -
Products: -
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arachidonoyl-CoA + 1-oleoyl-2-lysophosphatidylcholine
CoA + 1-oleoyl-2-arachidonoylphosphatidylcholine
C4B4E7
Substrates: -
Products: -
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arachidonoyl-CoA + 1-oleoyl-glycerol-3-phosphate
1-oleoyl-2-arachidonoyl-glycerol-3-phosphate + CoA
-
Substrates: -
Products: -
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arachidonoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-arachidonoyl-sn-glycerol 3-phosphate
arachidonoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine
CoA + 1-oleoyl-2-arachidonoylphosphatidylcholine
Substrates: -
Products: -
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arachidonoyl-CoA + 1-palmitoyl-2-lysophosphatidylinositol
CoA + 1-palmitoyl-2-arachidonoylphosphatidylinositol
C4B4E7
Substrates: -
Products: -
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arachidonoyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-arachidonoyl-sn-glycerol 3-phosphate
Substrates: slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
Products: -
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arachidonoyl-CoA + 1-palmitoyl-sn-lysophosphatidylcholine
CoA + 1-palmitoyl-2-arachidonoylphosphatidylcholine
Substrates: -
Products: -
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arachidonoyl-CoA + 1-stearoyl-2-lysophosphatidic acid
CoA + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: -
Products: -
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arachidonoyl-CoA + 1-stearoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-stearoyl-sn-glycerol 3-phosphate
Substrates: slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
Products: -
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arachidonoyl-CoA + 1-stearoyl-sn-lysophosphatidylcholine
CoA + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphocholine
Substrates: -
Products: -
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arachidonoyl-CoA + oleoyl-lysophosphatidic acid
CoA + 2-arachidonoyl-1-oleoyl-sn-glycerol 3-phosphate
arachidoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-arachidoyl-lysophosphatidic acid
Substrates: very low activity
Products: -
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arachidoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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arachidoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 2-arachidoyl-1-oleoyl-sn-glycerol 3-phosphate
behenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-behenoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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capryl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-capryl-sn-glycerol 3-phosphate
cis-11-eicosenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-cis-11 eicosenoyl-sn-glycerol 3-phosphate
docosahexaenoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-docosahexaenoyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: best substrates
Products: -
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eicosapentaenoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-eicosapentaenoyl-lysophosphatidic acid
eicosapentaenoyl-CoA + oleoyl-lysophosphatidic acid
CoA + 2-eicosapentaenoyl-1-oleoyl-sn-glycerol 3-phosphate
eicosatetraenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-eicosatetraenoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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erucoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-erucoyl-sn-glycerol 3-phosphate
erucoyl-CoA + 1-erucoyl-sn-glycerol-3-phosphate
CoA + 1,2-dierucoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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gondoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-gondoyl-sn-glycerol 3-phosphate
-
Substrates: gondoyl-CoA is utilized less efficiently for the reaction than oleoyl-CoA
Products: -
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heptadecanoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-heptadecanoyl-sn-glycerol 3-phosphate
lauroyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-lauroyl-lysophosphatidic acid
Substrates: -
Products: -
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lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate
lauroyl-CoA + 1-lauroyl-sn-glycerol 3-phosphate
CoA + 1,2-dilauroyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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lauroyl-CoA + 1-oleoyl-2-lysophosphatidic acid
CoA + 2-lauroyl-1-oleoyl-sn-glycerol 3-phosphate
lignoceroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lignoceroyl-sn-glycerol 3-phosphate
linolenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linolenoyl-sn-glycerol 3-phosphate
linoleoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-linoleoyl-lysophosphatidic acid
linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
linoleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-linoleoyl-sn-glycerol 3-phosphate
linoleoyl-CoA + oleoyl-lysophosphatidic acid
CoA + 2-linoleoyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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myristoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-myristoyl-lysophosphatidic acid
myristoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-myristoyl-sn-glycerol 3-phosphate
myristoyl-CoA + 1-myristoyl-sn-glycerol 3-phosphate
CoA + 1,2-dimyristoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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myristoyl-CoA + 1-oleoyl-2-lysophosphatidic acid
CoA + 1-oleoyl-2-stearoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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myristoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-myristoyl-sn-glycerol 3-phosphate
-
Substrates: about 25% of the activity with oleoyl-CoA by AGPAT10/GPAT3
Products: -
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myristoyl-[acyl-carrier protein] + 1-acyl-sn-glycerol 3-phosphate
acyl-carrier protein + 1-acyl-2-myristoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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oleoyl-ACP + sn-1-oleoylglycerol 3-phosphate
ACP + sn-1,2-dioleoylglycerol 3-phosphate
-
Substrates: microsomal fractions from developing, transgenic seeds but not of untransformed plants
Products: -
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oleoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-oleoyl-lysophosphatidic acid
oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
oleoyl-CoA + 1-arachidonoyl-sn-glycerol 3-phosphate
CoA + 1-arachidonoyl-2-oleoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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oleoyl-CoA + 1-arachidonoyl-sn-lysophosphatidylcholine
CoA + 1-arachidonoyl-2-oleoyl-sn-glycero-3-phosphocholine
Substrates: -
Products: -
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oleoyl-CoA + 1-erucoyl-sn-glycerol 3-phosphate
CoA + 1-erucoyl-2-oleoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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oleoyl-CoA + 1-oleoyl-2-lysophosphatidylcholine
CoA + 1,2-dioleoyl-sn-glycero-3-phosphocholine
oleoyl-CoA + 1-oleoyl-2-lysophosphatidylethanolamine
CoA + 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
-
Substrates: about 10% of the activity with 1-oleoyl-2-lysophopshatidic acid by AGPAT10/GPAT3
Products: -
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oleoyl-CoA + 1-oleoyl-2-lysophosphatidylglycerol
CoA + 1,2-dioleoyl-sn-glycero-3-phosphate
-
Substrates: about 10% of the activity with 1-oleoyl-2-lysophopshatidic acid by AGPAT10/GPAT3
Products: -
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oleoyl-CoA + 1-oleoyl-2-lysophosphatidylinositol
CoA + 1,2-dioleoyl-sn-phosphatidylinositol
oleoyl-CoA + 1-oleoyl-2-lysophosphatidylserine
CoA + 1,2-dioleoyl-sn-glycerol-3-phospho-L-serine
-
Substrates: about 10% of the activity with 1-oleoyl-2-lysophopshatidic acid by AGPAT10/GPAT3
Products: -
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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
oleoyl-CoA + 1-oleoyl-sn-glycerol-3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine
CoA + 1,2-dioleoyl-sn-lysophosphatidylcholine
Substrates: low activity, cf. EC 2.3.1.23. Slc1 has no detectable reverse reaction towards PtdCho substrate
Products: -
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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
oleoyl-CoA + 1-palmitoyl-sn-lysophosphatidylcholine
CoA + 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
Substrates: -
Products: -
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oleoyl-CoA + 1-stearoyl-sn-lysophosphatidylcholine
CoA + 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine
Substrates: -
Products: -
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oleoyl-CoA + lysophosphatidic acid
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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oleoyl-CoA + oleoyl-lysophosphatidic acid
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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palmitoleoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-palmitoleoyl-lysophosphatidic acid
Substrates: -
Products: -
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palmitoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoleoyl-sn-glycerol 3-phosphate
palmitoleoyl-CoA + 1-oleoyl-2-lysophosphatidic acid
CoA + 1-oleoyl-2-palmitoleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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palmitoleoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-palmitoleoyl-lysophosphatidic acid
Substrates: -
Products: -
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palmitoyl-ACP + 1-acyl-sn-glycerol 3-phosphate
ACP + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
palmitoyl-CoA + 1-(9Z)-octa-9-decenyl-lysophosphatidic acid
CoA + 1-(9Z)-octa-9-decenyl-2-palmitoyl-lysophosphatidic acid
Substrates: -
Products: -
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palmitoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-palmitoyl-lysophosphatidic acid
Substrates: -
Products: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
palmitoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-palmitoyl-sn-glycerol 3-phosphate
palmitoyl-[acyl carrier protein] + 1-acyl-sn-glycerol 3-phosphate
acyl carrier protein + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
pentadecanoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-pentadecanoyl-sn-glycerol 3-phosphate
stearoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-stearoyl-lysophosphatidic acid
stearoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-stearoyl-sn-glycerol 3-phosphate
stearoyl-CoA + 1-oleoyl-2-lysophosphatidic acid
CoA + 1-oleoyl-2-stearoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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stearoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-stearoyl-sn-glycerol 3-phosphate
additional information
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-
acyl-ACP + 1-acyl-sn-glycerol 3-phosphate
ACP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: negligible
Products: -
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acyl-ACP + 1-acyl-sn-glycerol 3-phosphate
ACP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: catalyzes acylation of position 2 hydroxyl-group, acyl-donor: highly specific for palmitoyl-ACP preferred to oleoyl-ACP, acyl-acceptors are: 1-oleoyl-sn-glycerol 3-phosphate, which is the best and 1-palmitoyl-sn-glycerol 3-phosphate
Products: -
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acyl-ACP + 1-acyl-sn-glycerol 3-phosphate
ACP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: negligible
Products: -
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acyl-ACP + 1-acyl-sn-glycerol 3-phosphate
ACP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: catalyzes acylation of position 2 hydroxyl-group, acyl-donor: highly specific for palmitoyl-ACP preferred to oleoyl-ACP, acyl-acceptors are: 1-oleoyl-sn-glycerol 3-phosphate, which is the best and 1-palmitoyl-sn-glycerol 3-phosphate
Products: -
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acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
Substrates: -
Products: -
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acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
Substrates: AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, acyl-CoA specificity, overview
Products: -
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acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
Substrates: -
Products: -
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acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
Substrates: AGPAT1 shows strict acyl acceptor specificity for lysophosphatidic acid, acyl-CoA specificity, overview
Products: -
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acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
Substrates: -
Products: -
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acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
Substrates: -
Products: -
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: i.e. lysophosphatidic acid
Products: i.e. phosphatidic acid
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
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Substrates: pivotal enzyme controlling the metabolic flow of lysophosphatidic acid into different phosphatidic acids in diverse tissues, enzyme is essential in embryo development
Products: -
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
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Substrates: the enzyme is active towards acyl-CoAs of chain length C-8 to C-18
Products: -
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: i.e. lysophosphatidic acid
Products: i.e. phosphatidic acid
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: i.e. phosphatidic acid
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
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Substrates: i.e. lysophosphatidic acid, highly specific for 1-acyl-sn-glycerol 3-phosphate, catalyzes acylation of position 2 hydroxyl-group
Products: i.e. phosphatidic acid
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
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Substrates: acyl-donors are saturated and unsaturated fatty acyl-CoAs
Products: -
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
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Substrates: involved in phospholipid biosynthesis
Products: -
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: reduction in AGPAT2 activity underlies the loss of adipose tissue in congenital generalized lipodystrophy
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: AGPAT2 catalyzes acylation of lysophosphatidic acid to phosphatidic acid, a precursor for both triacylglycerol and phospholipid synthesis, isozyme AGPAT2 plays a regulatory role in adipocyte differentiation
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: the enzyme catalyzes the transfer of the fatty acid from an acyl donor to the sn-2-position of lysophosphatidic acid
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: the enzyme catalyzes the transfer of the fatty acid from an acyl donor to the sn-2-position of lysophosphatidic acid
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: activity and expression pattern of AGPAT9 in lung and spleen implicates role in the biosynthesis of phospholipids and triglycerides in these tissues
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: acylation of lysophosphatidic acid to phosphatidic acid, precursor for triacylglycerol and phospholipid synthesis
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: cloning and characterization of isoform AGPAT9
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: substrate preference analyzed, assays performed with different acyl donors
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: the enzyme catalyzes the second acylations in the glycerol-3-phosphate pathway
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: the preferred substrate of LPAAT is 18:2-CoA
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: recombinant enzyme can catalyse ATP-independent acyl-CoA synthetic activity and CoA-dependent transacylation activity. Acyl-CoA synthetase is not involved in the process
Products: -
r
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: i.e. lysophosphatidic acid
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: the expression of AGPATs is linked to skin barrier requirements
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: the enzyme catalyzes the transfer of the fatty acid from an acyl donor to the sn-2-position of lysophosphatidic acid
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: i.e. lysophosphatidic acid, the recombinant CGI-58 shows preference for arachidonoyl-CoA and oleoyl-CoA, and slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: preferred donor substrate is arachidonoyl-CoA, no activity with oleoyl-CoA, strong activity with arachidonoyl-CoA and palmitoyl-lysophosphatidic acid, stearoyl-lysophosphatidic acid, oleoyl-lysophosphatidic acid, and octadecenyl-lysophosphatidic acid as acceptors
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: the enzyme has high acyl-CoA specificity for polyunsaturated fatty acyl-CoA, especially docosahexaenoyl-CoA
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: preferred donor substrate is arachidonoyl-CoA, no activity with oleoyl-CoA, strong activity with arachidonoyl-CoA and palmitoyl-lysophosphatidic acid, stearoyl-lysophosphatidic acid, oleoyl-lysophosphatidic acid, and octadecenyl-lysophosphatidic acid as acceptors
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: with 1 to 5 double bonds
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
KX256278
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
KX256278
Substrates: enzyme LPAAT catalyzes lysophosphatidic acid to yield phosphatidic acid by acylation of the sn-2 position of glycerol 3-phosphate. LPAAT is able to discriminate acyl groups with different chain lengths and possesses a selectivity and specificity for unsaturated C18 acyl groups in traditional oil seed crops
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: i.e. lysophosphatidic acid, highly specific for 1-acyl-sn-glycerol 3-phosphate, catalyzes acylation of position 2 hydroxyl-group
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: unsaturated preferred
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: pronounced specificities and selectivities for unsaturated C18-CoA thioesters
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: involved in phospholipid biosynthesis
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: C-14 to C-22
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: acyl-donors are saturated and unsaturated fatty acyl-CoAs
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: omega-3 and omega-6 polyunsaturated fatty acyl-CoAs
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: 1 to 6 double bonds
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: with 1 to 5 double bonds
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: with 1 to 5 double bonds
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: unsaturated preferred
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: monoenic and dienic acyl-CoA thioesters
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: C-16, C-18, C-20 acyl-CoAs and C-22 acyl-CoA
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: involved in phospholipid biosynthesis
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: i.e. lysophosphatidic acid, highly specific for 1-acyl-sn-glycerol 3-phosphate, catalyzes acylation of position 2 hydroxyl-group
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: effect of substrate concentration
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: the enzyme utilizes saturated and unsaturated acyl-CoAs at comparable rates
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: acyltranferase activity by Slc1p and Slc4p
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: Slc1p and Slc4p both active as acyltransferases, involved in fatty acid exchange of mature glycerophospholipids
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: glycerophospholipid profile similar between Slc1p and Slc4p
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: i.e. lysophosphatidic acid, highly specific for 1-acyl-sn-glycerol 3-phosphate, catalyzes acylation of position 2 hydroxyl-group
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: involved in phospholipid biosynthesis
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: i.e. phosphatidic acid
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: CoA esters of unsaturated 16- and 18-carbon fatty acids are the best substrates, followed by those saturated 14-, 16-, and 18-carbon acids, and the unsaturated 20-carbon acids
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: C-14 to C-22
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: acyl-donors are saturated and unsaturated fatty acyl-CoAs
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: omega-3 and omega-6 polyunsaturated fatty acyl-CoAs
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: with 1 to 5 double bonds
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
-
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidylethanolamine
CoA + 1-oleoyl-2-acyl-lysophosphatidylethanolamine
Substrates: low activity
Products: -
?
acyl-CoA + 1-oleoyl-lysophosphatidylethanolamine
CoA + 1-oleoyl-2-acyl-lysophosphatidylethanolamine
Substrates: low activity
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-acyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-acyl-sn-glycerol 3-phosphate
Substrates: low activity
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
-
Substrates: 1-oleoyl-sn-glycerol 3-phosphate is the best acceptor
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
r
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
acyl-CoA + 2-acyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: the enzyme does not acylate 2-acyl-sn-glycerol 3-phosphate
Products: -
?
acyl-CoA + 2-acyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: the enzyme does not acylate 2-acyl-sn-glycerol 3-phosphate
Products: -
?
acyl-CoA + 2-acyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: the rate of CoA-liberation is much lower than with 1-acyl-sn-glycerol 3-phosphate
Products: -
?
acyl-CoA + 2-acyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: the enzyme does not acylate 2-acyl-sn-glycerol 3-phosphate
Products: -
?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
-
Substrates: -
Products: -
?
acyl-[acyl-carrier protein] + 1-acyl-sn-glycerol 3-phosphate
ACP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: involved in phospholipid biosynthesis in chloroplasts
Products: -
?
acyl-[acyl-carrier protein] + 1-acyl-sn-glycerol 3-phosphate
ACP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Substrates: involved in phospholipid biosynthesis in chloroplasts
Products: -
?
acyl-[acyl-carrier protein] + 1-acyl-sn-glycerol 3-phosphate
acyl-carrier protein + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
acyl-[acyl-carrier protein] + 1-acyl-sn-glycerol 3-phosphate
acyl-carrier protein + 1,2-diacyl-sn-glycerol 3-phosphate
Substrates: the enzyme has a high substrate specificity toward 14:0-ACP
Products: -
?
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
?
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: -
Products: -
?
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: -
Products: -
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arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
Substrates: arachidonoyl-CoA is a poor substrate
Products: -
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arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
Substrates: arachidonoyl-CoA is a poor substrate
Products: -
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arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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arachidonoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-arachidonoyl-sn-glycerol 3-phosphate
Substrates: about half of the rate with oleoyl-CoA
Products: -
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arachidonoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-arachidonoyl-sn-glycerol 3-phosphate
Substrates: and oleoyl-CoA, preferred substrates
Products: -
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arachidonoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-arachidonoyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: minor substrate
Products: -
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arachidonoyl-CoA + oleoyl-lysophosphatidic acid
CoA + 2-arachidonoyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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arachidonoyl-CoA + oleoyl-lysophosphatidic acid
CoA + 2-arachidonoyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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arachidoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 2-arachidoyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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arachidoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 2-arachidoyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
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capryl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-capryl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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capryl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-capryl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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cis-11-eicosenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-cis-11 eicosenoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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cis-11-eicosenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-cis-11 eicosenoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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eicosapentaenoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-eicosapentaenoyl-lysophosphatidic acid
Substrates: -
Products: -
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eicosapentaenoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-eicosapentaenoyl-lysophosphatidic acid
Substrates: -
Products: -
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eicosapentaenoyl-CoA + oleoyl-lysophosphatidic acid
CoA + 2-eicosapentaenoyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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eicosapentaenoyl-CoA + oleoyl-lysophosphatidic acid
CoA + 2-eicosapentaenoyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
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erucoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-erucoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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erucoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-erucoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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erucoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-erucoyl-sn-glycerol 3-phosphate
-
Substrates: erucoyl-CoA is a poor substrate
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heptadecanoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-heptadecanoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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heptadecanoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-heptadecanoyl-sn-glycerol 3-phosphate
Substrates: about half of the rate with oleoyl-CoA
Products: -
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lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate
-
Substrates: transgenic seeds: preferred substrate
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lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate
-
Substrates: lauroyl-CoA is a poor substrate
Products: -
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lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate
-
Substrates: lauroyl-CoA is a poor substrate
Products: -
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lauroyl-CoA + 1-oleoyl-2-lysophosphatidic acid
CoA + 2-lauroyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
Products: -
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lauroyl-CoA + 1-oleoyl-2-lysophosphatidic acid
CoA + 2-lauroyl-1-oleoyl-sn-glycerol 3-phosphate
Substrates: the enzyme shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. Saturated fatty acyl-CoAs, especially those with a carbon chain length of 14 or longer, serve as poor fatty acyl donors. The enzyme accepts lysophosphatidic acid having either unsaturated or saturated acyl chains. It shows little activity towards sn-glycerol 3-phosphate and lysophospholipids with head groups
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lignoceroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lignoceroyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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lignoceroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lignoceroyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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linolenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linolenoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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linolenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linolenoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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linolenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linolenoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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linoleoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-linoleoyl-lysophosphatidic acid
Substrates: -
Products: -
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linoleoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-linoleoyl-lysophosphatidic acid
Substrates: -
Products: -
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linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
-
Substrates: linoleoyl-CoA is a good substrate but is utilized less efficiently than oleoyl-CoA
Products: -
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linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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linoleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-linoleoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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linoleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-linoleoyl-sn-glycerol 3-phosphate
Substrates: about half of the rate with oleoyl-CoA
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linoleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-linoleoyl-sn-glycerol 3-phosphate
Substrates: linoleoyl-CoA is second best acyl-CoA substrate
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linoleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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myristoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-myristoyl-lysophosphatidic acid
Substrates: -
Products: -
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myristoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-myristoyl-lysophosphatidic acid
Substrates: low activity
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myristoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-myristoyl-sn-glycerol 3-phosphate
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Substrates: myristoyl-CoA is a poor substrate
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myristoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-myristoyl-sn-glycerol 3-phosphate
Substrates: -
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myristoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-myristoyl-sn-glycerol 3-phosphate
-
Substrates: -
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myristoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-myristoyl-sn-glycerol 3-phosphate
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Substrates: myristoyl-CoA is a poor substrate
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oleoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-oleoyl-lysophosphatidic acid
Substrates: -
Products: -
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oleoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-oleoyl-lysophosphatidic acid
Substrates: -
Products: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
Products: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
Substrates: i.e. lysophosphatidic acid
Products: i.e. phosphatidic acid
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
Substrates: twice as good as palmitoyl-CoA
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
Substrates: high selectivity for oleate
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
Substrates: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
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Substrates: -
Products: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
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Substrates: oleoyl-CoA is the best substrate, both membrane-bound and partially purified enzyme
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
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Substrates: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
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Substrates: is the most effective acyl donor
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
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Substrates: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
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Substrates: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
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Substrates: -
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oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
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Substrates: -
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oleoyl-CoA + 1-oleoyl-2-lysophosphatidylcholine
CoA + 1,2-dioleoyl-sn-glycero-3-phosphocholine
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Substrates: about 10% of the activity with 1-oleoyl-2-lysophopshatidic acid by AGPAT10/GPAT3
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oleoyl-CoA + 1-oleoyl-2-lysophosphatidylcholine
CoA + 1,2-dioleoyl-sn-glycero-3-phosphocholine
Substrates: -
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oleoyl-CoA + 1-oleoyl-2-lysophosphatidylinositol
CoA + 1,2-dioleoyl-sn-phosphatidylinositol
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Substrates: -
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oleoyl-CoA + 1-oleoyl-2-lysophosphatidylinositol
CoA + 1,2-dioleoyl-sn-phosphatidylinositol
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Substrates: about 10% of the activity with 1-oleoyl-2-lysophopshatidic acid by AGPAT10/GPAT3
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oleoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
Substrates: -
Products: -
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oleoyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1,2-dioleoyl-sn-lysophosphatidic acid
Substrates: preferred substrate. Slc1 has a very high capacity of reversibility towards the PtdOH substrate
Products: -
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oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
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Substrates: assayed with BAT2 protein
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oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
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Substrates: oleoyl-CoA and 1-oleoyl-sn-glycerol 3-phosphate are the preferred substrates of AGPAT10/GPAT3
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oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
Substrates: both substrates are preferred
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oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
Substrates: both substrates are preferred
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oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
Substrates: both substrates are preferred
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oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
Substrates: -
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oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
Substrates: and arachidonoyl-CoA, preferred substrates. Slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
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oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
C4B4E7
Substrates: minor substrate
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oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
Substrates: oleoyl-CoA is used at higher rates than palmitoyl-CoA. 1-oleoyl-sn-glycerol 3-phosphate is a more efficient substrate than 1-palmitoyl-sn-glycerol 3-phosphate. From mixtures of oleoyl- and palmitoyl-CoA, the enzyme selectively transfers oleic acid to the C2 position of 1-palmitoyl- and 1-oleoyl-sn-glycerol 3-phosphate
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oleoyl-CoA + 1-oleoyl-sn-glycerol-3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
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Substrates: -
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oleoyl-CoA + 1-oleoyl-sn-glycerol-3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
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Substrates: substrate preference higher for oleoyl-CoA than for palmitoyl-CoA and stearoyl-CoA
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oleoyl-CoA + 1-oleoyl-sn-glycerol-3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
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Substrates: substrate preference higher for oleoyl-CoA than for palmitoyl-CoA and stearoyl-CoA
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oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
Substrates: -
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oleoyl-CoA + 1-oleoyl-sn-lysophosphatidylethanolamine
CoA + 1,2-dioleoyl-sn-lysophosphatidylethanolamine
Substrates: lower activity, cf. EC 2.3.1.121
Products: -
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oleoyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
Substrates: -
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oleoyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
Substrates: oleoyl-CoA is used at higher rates than palmitoyl-CoA. 1-oleoyl-sn-glycerol 3-phosphate is a more efficient substrate than 1-palmitoyl-sn-glycerol 3-phosphate. From mixtures of oleoyl- and palmitoyl-CoA, the enzyme selectively transfers oleic acid to the C2 position of 1-palmitoyl- and 1-oleoyl-sn-glycerol 3-phosphate
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palmitoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoleoyl-sn-glycerol 3-phosphate
Substrates: palmitoleoyl-CoA is a good substrate
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palmitoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoleoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoleoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoleoyl-sn-glycerol 3-phosphate
-
Substrates: -
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palmitoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoleoyl-sn-glycerol 3-phosphate
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Substrates: palmitoleoyl-CoA is a good substrate but is utilized less efficiently than oleoyl-CoA
Products: -
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palmitoyl-ACP + 1-acyl-sn-glycerol 3-phosphate
ACP + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
Substrates: -
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palmitoyl-ACP + 1-acyl-sn-glycerol 3-phosphate
ACP + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: maximum activity is obtained with palmitoyl-CoA at a concentration of 0.002-0.003 mM
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: preferred acyl donor substrate
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: palmitoyl-CoA is the best substrate
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: acyltransferase motifs I-IV analyzed by sidechain modification, substrate accessibility to the catalytic domain analyzed by competition assay
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: palmitoyl-CoA is a poor substrate
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: palmitoyl-CoA is a poor substrate
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: substrate preference lower than for oleoyl-CoA
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: palmitoyl-CoA is a poor substrate
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: assayed with BAT2 protein, palmitoyl-CoA is the preferred substrate
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palmitoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-palmitoyl-sn-glycerol 3-phosphate
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Substrates: about 25% of the activity with oleoyl-CoA by AGPAT10/GPAT3
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palmitoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: about 40% of the rate with oleoyl-CoA
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palmitoyl-[acyl carrier protein] + 1-acyl-sn-glycerol 3-phosphate
acyl carrier protein + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-[acyl carrier protein] + 1-acyl-sn-glycerol 3-phosphate
acyl carrier protein + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-[acyl carrier protein] + 1-acyl-sn-glycerol 3-phosphate
acyl carrier protein + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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palmitoyl-[acyl carrier protein] + 1-acyl-sn-glycerol 3-phosphate
acyl carrier protein + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
Substrates: -
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pentadecanoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-pentadecanoyl-sn-glycerol 3-phosphate
Substrates: 50% of the rate with oleoyl-CoA and linoleoyl-CoA
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pentadecanoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-pentadecanoyl-sn-glycerol 3-phosphate
Substrates: rate is similar to oleoyl-CoA and linoleoyl-CoA
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stearoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-stearoyl-lysophosphatidic acid
Substrates: -
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stearoyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1-acyl-2-stearoyl-lysophosphatidic acid
Substrates: very low activity
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stearoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-stearoyl-sn-glycerol 3-phosphate
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Substrates: -
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stearoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-stearoyl-sn-glycerol 3-phosphate
Substrates: -
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stearoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-stearoyl-sn-glycerol 3-phosphate
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Substrates: -
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stearoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-stearoyl-sn-glycerol 3-phosphate
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Substrates: stearoyl-CoA is a poor substrate
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stearoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-stearoyl-sn-glycerol 3-phosphate
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Substrates: stearoyl-CoA is a poor substrate
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stearoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-stearoyl-sn-glycerol 3-phosphate
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Substrates: about 25% of the activity with oleoyl-CoA by AGPAT10/GPAT3
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stearoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-stearoyl-sn-glycerol 3-phosphate
Substrates: about 40% of the rate with oleoyl-CoA
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additional information
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Substrates: the endoplasmic reticulum-located LPAT2 is essential for female but not male gametophyte development in Arabidopsis thaliana, LPAT2 co-localizes with calreticulin in the endoplasmic reticulum
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Substrates: the endoplasmic reticulum-located LPAT2 is essential for female but not male gametophyte development in Arabidopsis thaliana, LPAT2 co-localizes with calreticulin in the endoplasmic reticulum
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additional information
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Substrates: the endoplasmic reticulum-located LPAT2 is essential for female but not male gametophyte development in Arabidopsis thaliana, LPAT2 co-localizes with calreticulin in the endoplasmic reticulum
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additional information
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Substrates: the endoplasmic reticulum-located LPAT2 is essential for female but not male gametophyte development in Arabidopsis thaliana, LPAT2 co-localizes with calreticulin in the endoplasmic reticulum
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additional information
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Substrates: the endoplasmic reticulum-located LPAT2 is essential for female but not male gametophyte development in Arabidopsis thaliana, LPAT2 co-localizes with calreticulin in the endoplasmic reticulum
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additional information
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Substrates: the endoplasmic reticulum-located LPAT2 is essential for female but not male gametophyte development in Arabidopsis thaliana, LPAT2 co-localizes with calreticulin in the endoplasmic reticulum
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additional information
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Substrates: comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and tiacylglycerols, overview
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additional information
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Substrates: 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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Substrates: no acyl-donors are butyryl-CoA and hexanoyl-CoA
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Substrates: the chain length specificity of the enzyme in decreasing order is as follows: C16, C14, C12, C10, C8
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Substrates: 1-palmitoyl- and 1-oleoyl-sn-glycerol 3-phosphate are probably the substrates for the enzyme in vivo, since palmitic and oleic acids are the major fatty acid components at the sn-1 position of cow milk triacylglycerols. The specificity of the enzyme plays a major role in determining the fatty acid composition at the sn-2 position of cow milk triacylglycerols, though the influence of other factors such as the in vivo concentration of the acyl-CoAs and the specificities of the monoacylglycerol acyltransferases cannot be ruled out
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Substrates: the enzyme controls phosphatidic acid biosynthesis in the plastid
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additional information
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Substrates: comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and tiacylglycerols, overview
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additional information
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Substrates: 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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Substrates: the broad substrate specificity of acyltransferase CT775 provides the organism with the capacity to incorporate straight-chain and bacterial specific branched-chain fatty acids. In vivo incorporation of 1-acyl-GPC in cells infected with Chlamydia trachomatis confirms the active remodeling of exogenous lipids that are translocated into the inclusions
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Substrates: the broad substrate specificity of acyltransferase CT775 provides the organism with the capacity to incorporate straight-chain and bacterial specific branched-chain fatty acids. In vivo incorporation of 1-acyl-GPC in cells infected with Chlamydia trachomatis confirms the active remodeling of exogenous lipids that are translocated into the inclusions
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Substrates: broad substrate specificity of acyltransferase CT775. It accepts both acyl-ACP and acyl-CoA as acyl donors and, 1- or 2-acyl isomers of lysophosphoplipids as acyl acceptors, cf. EC 2.3.1.62. CT775 is not exclusively a 2-acyl-GPL acyltransferase, 1-acyl-GPL acyltransferase. The transfer of NBD-C16-CoA to 1-acyl-GPC by hLPCAT1 is strongly reduced in the presence of MeC18-CoA. Although unsaturated C18 fatty acids are very abundant at the sn2 position of human PLs, MeC18-CoA is a stronger competitor than C18:1-CoA, possible preference of the bacterial enzyme for the palmitic chain compared to the stearic chain. MeC18-CoA is a substrate for CT775
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additional information
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Substrates: broad substrate specificity of acyltransferase CT775. It accepts both acyl-ACP and acyl-CoA as acyl donors and, 1- or 2-acyl isomers of lysophosphoplipids as acyl acceptors, cf. EC 2.3.1.62. CT775 is not exclusively a 2-acyl-GPL acyltransferase, 1-acyl-GPL acyltransferase. The transfer of NBD-C16-CoA to 1-acyl-GPC by hLPCAT1 is strongly reduced in the presence of MeC18-CoA. Although unsaturated C18 fatty acids are very abundant at the sn2 position of human PLs, MeC18-CoA is a stronger competitor than C18:1-CoA, possible preference of the bacterial enzyme for the palmitic chain compared to the stearic chain. MeC18-CoA is a substrate for CT775
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additional information
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Substrates: the broad substrate specificity of acyltransferase CT775 provides the organism with the capacity to incorporate straight-chain and bacterial specific branched-chain fatty acids. In vivo incorporation of 1-acyl-GPC in cells infected with Chlamydia trachomatis confirms the active remodeling of exogenous lipids that are translocated into the inclusions
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additional information
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Substrates: broad substrate specificity of acyltransferase CT775. It accepts both acyl-ACP and acyl-CoA as acyl donors and, 1- or 2-acyl isomers of lysophosphoplipids as acyl acceptors, cf. EC 2.3.1.62. CT775 is not exclusively a 2-acyl-GPL acyltransferase, 1-acyl-GPL acyltransferase. The transfer of NBD-C16-CoA to 1-acyl-GPC by hLPCAT1 is strongly reduced in the presence of MeC18-CoA. Although unsaturated C18 fatty acids are very abundant at the sn2 position of human PLs, MeC18-CoA is a stronger competitor than C18:1-CoA, possible preference of the bacterial enzyme for the palmitic chain compared to the stearic chain. MeC18-CoA is a substrate for CT775
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Substrates: the purified soluble recombinant CrLPAAT1 prefers C16:0-CoA over other acyl donors, whereas it shows broader substrate selectivity than the membrane-bound enzyme. Comparison of the wild-type CrLPAAT1 and the transmembrane domain-truncated enzyme revelas that the two transmembrane domains of CrLPAAT1 are involved in shaping its substrate preference for C16:0-CoA. The wild-type CrLPAAT1 can utilize C18:1 (n9)-LPA and C16:0- CoA to produce phosphatidic acid in a dosage-dependent manner. The transmembrane domains affect substrate selectivity, mechanism, detailed overview. The effect of two transmembrane domains of CrLPAAT1 is more dramatic on the selectivity on C16:0 than that on the other acyl-CoA substrates
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Substrates: acyl-CoAs containing 10:0, 12:0 and 14:0 acyl groups are the preferred acyl-donor substrates, acyl-ACPs are not utilized. There is a slight preference for 12:0-lysophosphatidic acid over 18:1-lysophosphatidic acid as acceptor substrate
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Substrates: expression of a 299-amino acid protein with enzyme activity alters the enzyme substrate specificity profile of transgenic canola seeds
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additional information
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Substrates: the enzyme has medium chain length substrate specificity appropriate to the biosynthesis of coconut oil
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additional information
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Substrates: comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and triacylglycerols, overview
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additional information
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Substrates: comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and triacylglycerols, overview
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additional information
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Substrates: 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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additional information
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Substrates: 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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Substrates: the enzyme can utilize various saturated and unsaturated acyl-CoAs at comparable rates, unsaturated fatty acyl-CoAs with cis- or trans-configuration are slightly better substrates than saturated acyl-CoAs
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Substrates: effect of acyl-CoA concentrations on enzyme reaction
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Substrates: description of a direct nonchromatographic assay for the enzyme
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Substrates: effect of variable ratios of oleoyl-CoA to palmitoyl-CoA on the reaction
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Substrates: 1-acyl-sn-glycerol 3-phosphate is readily acylated by unsaturated and saturated acyl-CoAs
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Substrates: lysophosphatidic acid, synthesized by EC 2.3.1.15, is utilized by the enzyme without prior mixing with the total membrane-associated pool of lysophosphatidic acid, and suggest a close proximity of the two enzymes in native E. coli membranes. This property of the acyltransferases is lost upon separation and reconstitution of enzyme activities
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Substrates: an introduced chimeric enzyme gene of E. coli alters the stereochemical composition of transgenic HEAR oil by preferentially directing cis-11 eicosenoic acid to its sn-2 position
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Substrates: effect of acyl-CoA concentrations on enzyme reaction
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additional information
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Substrates: 1-acyl-sn-glycerol 3-phosphate is readily acylated by unsaturated and saturated acyl-CoAs
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Substrates: substrate specificity, overview
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Substrates: substrate specificity, overview
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additional information
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Substrates: substrate specificity, overview
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additional information
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Substrates: substrate specificity, overview
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additional information
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Substrates: substrate specificity, overview
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Substrates: the enzyme has affinity for fatty acids of acyl chain lengths from 12 to 18 carbons with a slight dependence on the degree of saturation of the fatty acid. However the enzyme does not incorporate long chain fatty acids like C20:0 and C24:0 unless they are saturated
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Substrates: the enzyme has affinity for fatty acids of acyl chain lengths from 12 to 18 carbons with a slight dependence on the degree of saturation of the fatty acid. However the enzyme does not incorporate long chain fatty acids like C20:0 and C24:0 unless they are saturated
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Substrates: AGPAT8 shows moderate acyltransferase activity with oleoyl-CoA but lacks acyl-CoA:lysocardiolipin acyltransferase activity, human AGPAT2, acylation at the sn-2 position with wild-type AGPAT8 is similar for the LPA species containing oleoyl, linoleoyl, linolenoyl, and palmitoyl fatty acids at the sn-1 position, LPA species containing myristoyl, arachidoyl, arachidonoyl are not preferred, substrate specificity in vivo, overview
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Substrates: sn-1-acyl-lysophosphatidic acid and acly-CoA specficity, AGPAT8 is unable to use arachidonoyl-CoA as the acyl donor, overview
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Substrates: CGI-58 is a CoA-dependent lysophosphatidic acid acyltransferase that channels fatty acids released from the hydrolysis of stored triacylglycerols into phospholipids, overview
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Substrates: LPAAT3 regulates Golgi membrane tubule formation, trafficking, and structure by altering phospholipids and lysophospholipids. LPAAT3 alters ERGIC-53 distribution, a p58 receptor which is a lectin receptor that traffics between the cis-Golgi and the endoplasmic reticulum
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Substrates: substrate specificity of AGPAT10/GPAT3, overview
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Substrates: the CGI-58 carboxyl terminus includes a highly conserved consensus sequence, HXXXXD, required for acyltransferase activity
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Substrates: isoform AGPAT11 shows broad preferences for the lysophosphatidic acid containing saturated fatty acids C16:0-C18:0, including lysophosphatidic acid containing oleic acid. Lysophosphatidic acid with fatty acid C20:4 is acylated at only about one-half maximal rate compared with others. The preferred acyl donor follows the decreasing order of C18:1,C16:0, C18:2, C17:0. Fatty acyl-CoA consisting of short-chain fatty acids C8:0 to C13:0 and very long-chain from C20:0 to C26:0 are not substrates. Enzyme does not display glycerol-3-phosphate acyltransferase activity
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Substrates: isoform AGPAT11 shows broad preferences for the lysophosphatidic acid containing saturated fatty acids C16:0-C18:0, including lysophosphatidic acid containing oleic acid. Lysophosphatidic acid with fatty acid C20:4 is acylated at only about one-half maximal rate compared with others. The preferred acyl donor follows the decreasing order of C18:1,C16:0, C18:2, C17:0. Fatty acyl-CoA consisting of short-chain fatty acids C8:0 to C13:0 and very long-chain from C20:0 to C26:0 are not substrates. Enzyme does not display glycerol-3-phosphate acyltransferase activity
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Substrates: isoform AGPAT3 shows broad preference for lysophosphatidic acids containing saturated or unsaturated fatty acids C16:0-C20:4 and significant esterification of lysophosphatidylinositol in the presence of oleoyl-CoA
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Substrates: isoform AGPAT3 shows broad preference for lysophosphatidic acids containing saturated or unsaturated fatty acids C16:0-C20:4 and significant esterification of lysophosphatidylinositol in the presence of oleoyl-CoA
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Substrates: isoform AGPAT3 shows broad preference for lysophosphatidic acids containing saturated or unsaturated fatty acids C16:0-C20:4 and significant esterification of lysophosphatidylinositol in the presence of oleoyl-CoA
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Substrates: isoform AGPAT5 demonstrates significant acyltransferase activity toward lysophosphatidylethanolamine in the presence of oleoyl-CoA
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Substrates: isoform AGPAT5 demonstrates significant acyltransferase activity toward lysophosphatidylethanolamine in the presence of oleoyl-CoA
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Substrates: isoform AGPAT5 demonstrates significant acyltransferase activity toward lysophosphatidylethanolamine in the presence of oleoyl-CoA
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Substrates: no substrates: acyl-CoA with fatty acids shorter than C14:0 or longer than C20:0, whether saturated or unsaturated
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Substrates: no substrates: acyl-CoA with fatty acids shorter than C14:0 or longer than C20:0, whether saturated or unsaturated
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Substrates: no substrates: acyl-CoA with fatty acids shorter than C14:0 or longer than C20:0, whether saturated or unsaturated
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Substrates: no substrates: acyl-CoA with fatty acids shorter than C14:0 or longer than C20:0, whether saturated or unsaturated. Isoform AGPAT2 is rather restrictive in using 1-oleoyl-sn-glycerol 3-phosphate as acceptor substrate
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Substrates: no substrates: acyl-CoA with fatty acids shorter than C14:0 or longer than C20:0, whether saturated or unsaturated. Isoform AGPAT2 is rather restrictive in using 1-oleoyl-sn-glycerol 3-phosphate as acceptor substrate
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Substrates: no substrates: acyl-CoA with fatty acids shorter than C14:0 or longer than C20:0, whether saturated or unsaturated. Isoform AGPAT2 is rather restrictive in using 1-oleoyl-sn-glycerol 3-phosphate as acceptor substrate
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Substrates: isozymes AGPAT3 and AGPAT5 have weak LPAAT activity compared to isozyme AGPAT2 and utilize other lysophospholipids as substrates
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Substrates: isozymes AGPAT3 and AGPAT5 have weak LPAAT activity compared to isozyme AGPAT2 and utilize other lysophospholipids as substrates
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Substrates: isozymes AGPAT3 and AGPAT5 have weak LPAAT activity compared to isozyme AGPAT2 and utilize other lysophospholipids as substrates
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Substrates: isozymes AGPAT3 and AGPAT5 have weak LPAAT activity compared to isozyme AGPAT2 and utilize other lysophospholipids as substrates
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Substrates: isozymes AGPAT3 and AGPAT5 have weak LPAAT activity compared to isozyme AGPAT2 and utilize other lysophospholipids as substrates
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Substrates: in vitro, the LPAAT activity of AGPAT1 has a broad specificity for acyl-CoAs, but also has ATP-independent acyl-CoA biosynthetic activity and CoA-dependent transacylation activity. Substrate specificity, overview
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Substrates: in vitro, the LPAAT activity of AGPAT1 has a broad specificity for acyl-CoAs, but also has ATP-independent acyl-CoA biosynthetic activity and CoA-dependent transacylation activity. Substrate specificity, overview
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Substrates: in vitro, the LPAAT activity of AGPAT1 has a broad specificity for acyl-CoAs, but also has ATP-independent acyl-CoA biosynthetic activity and CoA-dependent transacylation activity. Substrate specificity, overview
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Substrates: in vitro, the LPAAT activity of AGPAT1 has a broad specificity for acyl-CoAs, but also has ATP-independent acyl-CoA biosynthetic activity and CoA-dependent transacylation activity. Substrate specificity, overview
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Substrates: in vitro, the LPAAT activity of AGPAT1 has a broad specificity for acyl-CoAs, but also has ATP-independent acyl-CoA biosynthetic activity and CoA-dependent transacylation activity. Substrate specificity, overview
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Substrates: substrate specificity, overview. Besides lysophosphatidic acid, the isozyme also utilizes lyso-phosphocholine, -phosphoethanolamine and -phosphatidylserine as acyl acceptors. AGPAT3, AGPAT4, and AGPAT5 have LPAAT activity with oleoyl-CoA as the acyl donor, but also have LPLAT activity with a preference for polyunsaturated acyl-CoAs
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Substrates: substrate specificity, overview. Besides lysophosphatidic acid, the isozyme also utilizes lyso-phosphocholine, -phosphoethanolamine and -phosphatidylserine as acyl acceptors. AGPAT3, AGPAT4, and AGPAT5 have LPAAT activity with oleoyl-CoA as the acyl donor, but also have LPLAT activity with a preference for polyunsaturated acyl-CoAs
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Substrates: substrate specificity, overview. Besides lysophosphatidic acid, the isozyme also utilizes lyso-phosphocholine, -phosphoethanolamine and -phosphatidylserine as acyl acceptors. AGPAT3, AGPAT4, and AGPAT5 have LPAAT activity with oleoyl-CoA as the acyl donor, but also have LPLAT activity with a preference for polyunsaturated acyl-CoAs
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Substrates: substrate specificity, overview. Besides lysophosphatidic acid, the isozyme also utilizes lyso-phosphocholine, -phosphoethanolamine and -phosphatidylserine as acyl acceptors. AGPAT3, AGPAT4, and AGPAT5 have LPAAT activity with oleoyl-CoA as the acyl donor, but also have LPLAT activity with a preference for polyunsaturated acyl-CoAs
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Substrates: substrate specificity, overview. Besides lysophosphatidic acid, the isozyme also utilizes lyso-phosphocholine, -phosphoethanolamine and -phosphatidylserine as acyl acceptors. AGPAT3, AGPAT4, and AGPAT5 have LPAAT activity with oleoyl-CoA as the acyl donor, but also have LPLAT activity with a preference for polyunsaturated acyl-CoAs
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Substrates: comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and tiacylglycerols, overview
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Substrates: 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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Substrates: pLAT2 may be necessary only for specific storage triacylglycerol biosynthesis in developing seed
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Substrates: pLAT2 may be necessary only for specific storage triacylglycerol biosynthesis in developing seed
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Substrates: LPAT1 may be an enzyme required for membrane phospholipid biosynthesis in all tissues
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Substrates: LPAT1 may be an enzyme required for membrane phospholipid biosynthesis in all tissues
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Substrates: developmental and substrate specificity, overview
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Substrates: comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and tiacylglycerols, overview
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Substrates: 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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Substrates: comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and tiacylglycerols, overview
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Substrates: 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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C4B4E7
Substrates: substrate specificity, overview
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Substrates: substrate specificity, overview
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Substrates: the enzyme utilizes both saturated and unsaturated acyl-CoA as an acyl-donor but does not catalyse the transfer of acyl moiety to lysophosphatidylcholine or lyso-platelet-activating factor
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Substrates: lysophospholipids such as 1-acyl-sn-glycero-3-phosphocholine, 1-acyl-sn-glycero-3-phosphoethanolamine, 1-acyl-sn-glycero-3-phosphoinositol and lysoplatelet-activating factor do not serve as acyl acceptor substrates. Free fatty acids do not serve as acyl donors. The enzyme shows a broad specificity for acyl-CoAs
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Substrates: reverse reaction of the enzyme: desulfo-CoA and dephospho-COA do not serve as substrates for acyl-CoA synthesis
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Substrates: CGI-58 is a CoA-dependent lysophosphatidic acid acyltransferase that channels fatty acids released from the hydrolysis of stored triacylglycerols into phospholipids, overview
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Substrates: CGI-58 is a CoA-dependent lysophosphatidic acid acyltransferase that channels fatty acids released from the hydrolysis of stored triacylglycerols into phospholipids, overview
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C4B4E7
Substrates: mouse LPAAT3, previously known as mouse AGPAT3, possesses strong LPAAT activity and modest lysophosphatidylinositol acyltransferase activity with a clear preference for arachidonoyl-CoA as a donor, overview
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Substrates: mouse LPAAT3, previously known as mouse AGPAT3, possesses strong LPAAT activity and modest lysophosphatidylinositol acyltransferase activity with a clear preference for arachidonoyl-CoA as a donor, overview
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Substrates: the recombinant CoA-dependent His-tagged CGI-58 is active with lysophosphatidic acid, but not with other lysophospholipid or neutral glycerolipid acceptors
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Substrates: the recombinant CoA-dependent His-tagged CGI-58 is active with lysophosphatidic acid, but not with other lysophospholipid or neutral glycerolipid acceptors
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C4B4E7
Substrates: isoform LPAAT3 shows a clear preference for 18:1-lyso-PA as acyl acceptor and 22:6-CoA as acyl donor compared to other substrate combinations tested. The respective product sn-1-18:1-sn-2-22:6-phosphatidic acid is almost exclusively formed by LPAAT3. The enzyme shows Michaelis-Menten rate behavior toward 22:6-CoA in the presence of sn-1-18:1-lyso-phosphatidic acid
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Substrates: isoform LPAAT3 shows a clear preference for 18:1-lyso-PA as acyl acceptor and 22:6-CoA as acyl donor compared to other substrate combinations tested. The respective product sn-1-18:1-sn-2-22:6-phosphatidic acid is almost exclusively formed by LPAAT3. The enzyme shows Michaelis-Menten rate behavior toward 22:6-CoA in the presence of sn-1-18:1-lyso-phosphatidic acid
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Substrates: the enzyme interacts specifically with the phospholipid transfer protein StarD10 in vivo and in vitro as well as with one isoform of StarD7 but shows no interaction with StarD2/PC transfer protein
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Substrates: in vitro, the LPAAT activity of AGPAT1 has a broad specificity for acyl-CoAs, but also has ATP-independent acyl-CoA biosynthetic activity and CoA-dependent transacylation activity. Substrate specificity, overview
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Substrates: in vitro, the LPAAT activity of AGPAT1 has a broad specificity for acyl-CoAs, but also has ATP-independent acyl-CoA biosynthetic activity and CoA-dependent transacylation activity. Substrate specificity, overview
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C4B4E7
Substrates: substrate specificity, overview
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C4B4E7
Substrates: mouse LPAAT3, previously known as mouse AGPAT3, possesses strong LPAAT activity and modest lysophosphatidylinositol acyltransferase activity with a clear preference for arachidonoyl-CoA as a donor, overview
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Substrates: the enzyme interacts specifically with the phospholipid transfer protein StarD10 in vivo and in vitro as well as with one isoform of StarD7 but shows no interaction with StarD2/PC transfer protein
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Substrates: the enzyme uses preferably ACP-thioesters for the acylation of 1-acylglycerol 3-phosphate, the enzyme does not accept glycerol 3-phosphate as acyl-acceptor
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Substrates: the enzyme shows higher activities with acyl-CoA than with the corresponding acyl-(acyl carrier protein) thioesters, the enzyme is more active on unsaturated than on saturated acyl-CoA thioesters
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Substrates: no acyl-donors are coenzyme A derivatives
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Substrates: no acyl-donors are coenzyme A derivatives
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Substrates: no acyl acceptor is glycerol 3-phosphate
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Substrates: no acyl acceptor is glycerol 3-phosphate
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Substrates: the microsomal enzyme displays a specificity for unsaturated C18-CoA thioesters and this fatty-acid specificity is not altered in the course of the purification procedure
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Substrates: acyl-ACP rather than acyl-CoA is the physiological acyl donor for glycerolipid biosynthesis in chloroplasts
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Substrates: acyl-CoA thioesters can be considered as the physiological substrates of the microsomal enzyme
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Substrates: no acceptors are 1-acyl-sn-glycero-3-phosphoethanolamine, 1-acyl-sn-glycero-3-phosphomonomethylethanolamine, 1-acyl-sn-glycero-3-phosphodimethylethanolamine or 1-acyl-sn-glycero-3-phosphocholine
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Substrates: the enzyme exhibits a considerable selectivity for monoenoic and dienoic fatty acyl-CoA thioesters
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Substrates: the enzyme system shows relatively broad specificity for saturated and unsaturated fatty acids, with 14- to 20-carbon chains. Time courses fo the acylations of 1-acyl-glycerophosphate in the presence of equimolar mixtures of oleoyl-CoA and arachidonoyl-CoA
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Substrates: analysis of distribution of fatty acids at sn-positions of glycerol moiety of glycerolipids, overview
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Substrates: analysis of distribution of fatty acids at sn-positions of glycerol moiety of glycerolipids, overview
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Substrates: 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
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Substrates: no substrates: lysophosphatidyl choline, lysophosphatidyl ethanolamine, lysophosphatidyl glycerol, and lysophosphatidyl inositol
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Substrates: no substrates: lysophosphatidyl choline, lysophosphatidyl ethanolamine, lysophosphatidyl glycerol, and lysophosphatidyl inositol
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Substrates: 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
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Substrates: 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
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Substrates: 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
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Substrates: 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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Substrates: the enzyme has a substrate preference for the acyl donors with a polyunsaturated fatty acyl group, such as eicosapentaenoyl group. It shows almost no activity towards palmitoyl-CoA
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Substrates: the enzyme has a substrate preference for the acyl donors with a polyunsaturated fatty acyl group, such as eicosapentaenoyl group. It shows almost no activity towards palmitoyl-CoA
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Substrates: substrate specificity of isozyme SlPlsC1 towards fatty acyl-CoAs and lysophospholipids, overview. SlPlsC1 shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. The saturated acyl-CoAs, especially those with a carbon chain length of 14 or longer, served as poor fatty acyl donors. SlPlsC1 shows almost no activity towards palmitoyl-CoA. SlPlsC1 accepts lysophosphatidic acids (LPA) having either unsaturated or saturated acyl chains. It shows little activity towards glycerol 3-phosphate and lysophospholipids with head groups, thereby suggesting that SlPlsC1 is dedicated to the production of phosphatidic acid and is not involved in the acyl chain remodeling of phospholipids with a head group
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Substrates: substrate specificity of isozyme SlPlsC1 towards fatty acyl-CoAs and lysophospholipids, overview. SlPlsC1 shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. The saturated acyl-CoAs, especially those with a carbon chain length of 14 or longer, served as poor fatty acyl donors. SlPlsC1 shows almost no activity towards palmitoyl-CoA. SlPlsC1 accepts lysophosphatidic acids (LPA) having either unsaturated or saturated acyl chains. It shows little activity towards glycerol 3-phosphate and lysophospholipids with head groups, thereby suggesting that SlPlsC1 is dedicated to the production of phosphatidic acid and is not involved in the acyl chain remodeling of phospholipids with a head group
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Substrates: the enzyme has a substrate preference for the acyl donors with a polyunsaturated fatty acyl group, such as eicosapentaenoyl group. It shows almost no activity towards palmitoyl-CoA
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Substrates: the enzyme has a substrate preference for the acyl donors with a polyunsaturated fatty acyl group, such as eicosapentaenoyl group. It shows almost no activity towards palmitoyl-CoA
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Substrates: substrate specificity of isozyme SlPlsC1 towards fatty acyl-CoAs and lysophospholipids, overview. SlPlsC1 shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. The saturated acyl-CoAs, especially those with a carbon chain length of 14 or longer, served as poor fatty acyl donors. SlPlsC1 shows almost no activity towards palmitoyl-CoA. SlPlsC1 accepts lysophosphatidic acids (LPA) having either unsaturated or saturated acyl chains. It shows little activity towards glycerol 3-phosphate and lysophospholipids with head groups, thereby suggesting that SlPlsC1 is dedicated to the production of phosphatidic acid and is not involved in the acyl chain remodeling of phospholipids with a head group
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Substrates: substrate specificity of isozyme SlPlsC1 towards fatty acyl-CoAs and lysophospholipids, overview. SlPlsC1 shows high specificity towards the unsaturated fatty acyl-CoAs, among which those having multiple cis-double bonds (linoleoyl-, arachidonoyl-, and eicosapentaenoyl-CoAs) are more preferred substrates. The saturated acyl-CoAs, especially those with a carbon chain length of 14 or longer, served as poor fatty acyl donors. SlPlsC1 shows almost no activity towards palmitoyl-CoA. SlPlsC1 accepts lysophosphatidic acids (LPA) having either unsaturated or saturated acyl chains. It shows little activity towards glycerol 3-phosphate and lysophospholipids with head groups, thereby suggesting that SlPlsC1 is dedicated to the production of phosphatidic acid and is not involved in the acyl chain remodeling of phospholipids with a head group
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Substrates: fatty acid and phospholipid profiles, overview
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Substrates: the enzyme shows higher activities with acyl-CoA than with the corresponding acyl-(acyl carrier protein) thioesters, the enzyme is more active on unsaturated than on saturated acyl-CoA thioesters
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Substrates: no acyl-donors are coenzyme A derivatives
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Substrates: no acyl acceptor is glycerol 3-phosphate
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Substrates: the enzyme uses preferentially those acyl donors and acceptors, which contain oleate, specificity and selectivity experiments
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Substrates: the enzyme uses preferably ACP-thioesters for the acylation of 1-acylglycerol 3-phosphate, the enzyme does not accept glycerol 3-phosphate as acyl-acceptor
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Substrates: no acyl-donors are coenzyme A derivatives
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Substrates: no acyl acceptor is glycerol 3-phosphate
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Substrates: acyl-ACP rather than acyl-CoA is the physiological acyl donor for glycerolipid biosynthesis in chloroplasts
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Substrates: the enzyme has preference for cyclopropene fatty acids
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Substrates: the enzyme has preference for cyclopropene fatty acids
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Substrates: the enzyme system shows relatively broad specificity for saturated and unsaturated fatty acids, with 14- to 20-carbon chains. Time courses fo the acylations of 1-acyl-glycerophosphate in the presence of equimolar mixtures of oleoyl-CoA and arachidonoyl-CoA
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Substrates: TmPlsC expression in Escherichia coli strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0, analysis of acyl chain specificity, overview. Substrate tight association with the alphabeta catalytic domain is crucial to the function of the enzyme, an active site tunnel includes residues Tyr20, Ile21, Gly25, Ile49 and Phe52 from the N-terminal two-helix motif
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Substrates: TmPlsC expression in Escherichia coli strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0, analysis of acyl chain specificity, overview. Substrate tight association with the alphabeta catalytic domain is crucial to the function of the enzyme, an active site tunnel includes residues Tyr20, Ile21, Gly25, Ile49 and Phe52 from the N-terminal two-helix motif
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Substrates: TmPlsC expression in Escherichia coli strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0, analysis of acyl chain specificity, overview. Substrate tight association with the alphabeta catalytic domain is crucial to the function of the enzyme, an active site tunnel includes residues Tyr20, Ile21, Gly25, Ile49 and Phe52 from the N-terminal two-helix motif
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Substrates: TmPlsC expression in Escherichia coli strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0, analysis of acyl chain specificity, overview. Substrate tight association with the alphabeta catalytic domain is crucial to the function of the enzyme, an active site tunnel includes residues Tyr20, Ile21, Gly25, Ile49 and Phe52 from the N-terminal two-helix motif
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Substrates: TmPlsC expression in Escherichia coli strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0, analysis of acyl chain specificity, overview. Substrate tight association with the alphabeta catalytic domain is crucial to the function of the enzyme, an active site tunnel includes residues Tyr20, Ile21, Gly25, Ile49 and Phe52 from the N-terminal two-helix motif
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Substrates: comparison of the substrate specificities of enzymes from different species, positional analysis of fatty acids in seed oil and tiacylglycerols, overview
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additional information
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Substrates: 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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