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Literature summary for 2.3.1.51 extracted from

  • Lee, J.; Ridgway, N.
    Substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids (2020), Biochim. Biophys. Acta, 1865, 158438-158448 .
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Homo sapiens 5783
-
endoplasmic reticulum
-
Mus musculus 5783
-
lipid droplet
-
Homo sapiens 5811
-
mitochondrion
-
Homo sapiens 5739
-
additional information isozyme AGPAT3 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets Homo sapiens
-
-
additional information isozyme AGPAT5 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope and mitochondria. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets Homo sapiens
-
-
additional information seipin is colocalized with AGPAT2 and LIPIN-1 in the endoplasmic reticulum. A seipin-AGPAT2-LIPIN-1 complex may compartmentalize phosphatidic acid and diglyceride to enhance triglyceride synthesis Homo sapiens
-
-
nuclear envelope
-
Homo sapiens 5635
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + 1-acyl-lysophosphatidic acid Homo sapiens
-
CoA + 1,2-diacyl-lysophosphatidic acid
-
?
acyl-CoA + 1-acyl-lysophosphatidic acid Mus musculus
-
CoA + 1,2-diacyl-lysophosphatidic acid
-
?
additional information Homo sapiens isozymes AGPAT3 and AGPAT5 have weak LPAAT activity compared to isozyme AGPAT2 and utilize other lysophospholipids as substrates ?
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens O15120
-
-
Homo sapiens Q99943
-
-
Homo sapiens Q9NRZ5
-
-
Homo sapiens Q9NRZ7
-
-
Homo sapiens Q9NUQ2
-
-
Mus musculus O35083
-
-
Mus musculus Q8K3K7
-
-

Source Tissue

Source Tissue Comment Organism Textmining
adipocyte
-
Homo sapiens
-
adipocyte
-
Mus musculus
-
brain
-
Homo sapiens
-
heart
-
Homo sapiens
-
heart
-
Mus musculus
-
kidney
-
Homo sapiens
-
liver
-
Homo sapiens
-
liver
-
Mus musculus
-
lung
-
Homo sapiens
-
additional information analysis of tissue distribution of AGPAT2. AGPAT2 expression is increased during adipocyte differentiation and mutations cause congenital generalised lipodystrophy (CGL) type 1 Homo sapiens
-
additional information analysis of tissue distribution of AGPAT2. AGPAT2 expression is increased during adipocyte differentiation and mutations cause congenital generalised lipodystrophy (CGL) type 1 Mus musculus
-
additional information analysis of tissue distribution of AGPAT3 Homo sapiens
-
additional information analysis of tissue distribution of AGPAT5 Homo sapiens
-
additional information the mRNA for human AGPAT1 is ubiquitously expressed, analysis of tissue distribution of AGPAT1 Homo sapiens
-
additional information the mRNA for murine AGPAT1 is ubiquitously expressed, analysis of tissue distribution of AGPAT1 Mus musculus
-
pancreas
-
Homo sapiens
-
skeletal muscle
-
Homo sapiens
-
small intestine
-
Homo sapiens
-
testis
-
Homo sapiens
-
white adipose tissue
-
Homo sapiens
-
white adipose tissue
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-acyl-lysophosphatidic acid
-
Homo sapiens CoA + 1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-lysophosphatidic acid
-
?
acyl-CoA + 1-acyl-lysophosphatidic acid
-
Homo sapiens CoA + 1,2-diacyl-lysophosphatidic acid
-
?
acyl-CoA + 1-acyl-lysophosphatidic acid
-
Mus musculus CoA + 1,2-diacyl-lysophosphatidic acid
-
?
acyl-CoA + 1-acyl-lysophosphatidic acid AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, acyl-CoA specificity, overview Homo sapiens CoA + 1,2-diacyl-lysophosphatidic acid
-
?
acyl-CoA + 1-acyl-lysophosphatidic acid AGPAT1 shows strict acyl acceptor specificity for lysophosphatidic acid, acyl-CoA specificity, overview Mus musculus CoA + 1,2-diacyl-lysophosphatidic acid
-
?
alpha-linolenoyl-CoA + 1-acyl-lysophosphatidic acid
-
Homo sapiens CoA + 1-acyl-2-alpha-linolenoyl-lysophosphatidic acid
-
?
linoleoyl-CoA + 1-acyl-lysophosphatidic acid
-
Homo sapiens CoA + 1-acyl-2-linoleoyl-lysophosphatidic acid
-
?
additional information substrate specificity, overview Homo sapiens ?
-
-
additional information isozymes AGPAT3 and AGPAT5 have weak LPAAT activity compared to isozyme AGPAT2 and utilize other lysophospholipids as substrates Homo sapiens ?
-
-
additional information 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 Homo sapiens ?
-
-
additional information 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 Mus musculus ?
-
-
additional information 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 Homo sapiens ?
-
-
myristoyl-CoA + 1-acyl-lysophosphatidic acid
-
Homo sapiens CoA + 1-acyl-2-myristoyl-lysophosphatidic acid
-
?
oleoyl-CoA + 1-acyl-lysophosphatidic acid
-
Homo sapiens CoA + 1-acyl-2-oleoyl-lysophosphatidic acid
-
?
palmitoleoyl-CoA + 1-acyl-lysophosphatidic acid
-
Homo sapiens CoA + 1-acyl-2-palmitoleoyl-lysophosphatidic acid
-
?
palmitoyl-CoA + 1-acyl-lysophosphatidic acid
-
Homo sapiens CoA + 1-acyl-2-palmitoyl-lysophosphatidic acid
-
?
stearoyl-CoA + 1-acyl-lysophosphatidic acid
-
Homo sapiens CoA + 1-acyl-2-stearoyl-lysophosphatidic acid
-
?

Synonyms

Synonyms Comment Organism
1-acyl-sn-glycerol-3-phosphate acyltransferase
-
Homo sapiens
1-acyl-sn-glycerol-3-phosphate acyltransferase
-
Mus musculus
AGPAT1
-
Homo sapiens
AGPAT1
-
Mus musculus
AGPAT2
-
Homo sapiens
AGPAT2
-
Mus musculus
AGPAT3
-
Homo sapiens
AGPAT4
-
Homo sapiens
AGPAT5
-
Homo sapiens
LPAAT
-
Homo sapiens
LPAAT
-
Mus musculus
lysophosphatidic acid acyltransferase
-
Homo sapiens
lysophosphatidic acid acyltransferase
-
Mus musculus

Expression

Organism Comment Expression
Homo sapiens AGPAT2 expression is increased during adipocyte differentiation and mutations cause congenital generalised lipodystrophy (CGL) type 1 up

General Information

General Information Comment Organism
malfunction in cultured adipocytes, knockdown of AGPAT2 reduces TG synthesis and increased lyso-PA channeling into phospholipids Homo sapiens
malfunction in enzyme AGPAT2 defiecient mice, reduces TG synthesis and increased lyso-PA channeling into phospholipids is observed. In Agpat2-/- mouse liver, hepatic steatosis is driven by increased fatty acid synthesis and diversion of lyso-PA to TG and phospholipids by a mechanism independent of monoacylglycerol acyltransferase 1 (MGAT1) activity. The increase in phospholipid synthesis might be due to an alternate AGPAT-dependent pathway Mus musculus
metabolism the successive acylation of glycerol-3-phosphate (G3P) by glycerol-3-phosphate acyltransferases and acylglycerol-3-phosphate acyltransferases produces phosphatidic acid (PA), a precursor for CDP-diacylglycerol-dependent phospholipid synthesis. PA is further dephosphorylated by LIPINs to produce diacylglycerol (DG), a substrate for the synthesis of triglyceride (TG) by DG acyltransferases and a precursor for phospholipid synthesis via the CDP-choline and CDP-ethanolamine (Kennedy) pathways. The channeling of fatty acids into TG for storage in lipid droplets and secretion in lipoproteins or phospholipids for membrane biogenesis is dependent on isoform expression, activity and localization of G3P pathway enzymes, as well as dietary and hormonal and tissue-specific factors. Mechanisms that control partitioning of substrates into lipid products of the G3P pathway, glycerol-3-phosphate biosynthetic pathway, overview. Substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids Homo sapiens
metabolism the successive acylation of glycerol-3-phosphate (G3P) by glycerol-3-phosphate acyltransferases and acylglycerol-3-phosphate acyltransferases produces phosphatidic acid (PA), a precursor for CDP-diacylglycerol-dependent phospholipid synthesis. PA is further dephosphorylated by LIPINs to produce diacylglycerol (DG), a substrate for the synthesis of triglyceride (TG) by DG acyltransferases and a precursor for phospholipid synthesis via the CDP-choline and CDP-ethanolamine (Kennedy) pathways. The channeling of fatty acids into TG for storage in lipid droplets and secretion in lipoproteins or phospholipids for membrane biogenesis is dependent on isoform expression, activity and localization of G3P pathway enzymes, as well as dietary and hormonal and tissue-specific factors. Mechanisms that control partitioning of substrates into lipid products of the G3P pathway, glycerol-3-phosphate biosynthetic pathway, overview. Substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids Mus musculus
physiological function while isozymes AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, other isoforms utilize lyso-PC, -PE and -phosphatidylserine (PS) as acyl acceptors. Isozymes 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, suggesting a dual role in glycerolipid synthesis and remodeling Homo sapiens
physiological function while isozymes AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, other isoforms utilize lyso-PC, -PE and -phosphatidylserine (PS) as acyl acceptors. Isozymes 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, suggesting a dual role in glycerolipid synthesis and remodeling Mus musculus
physiological function while isozymes AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, other isoforms utilize lyso-PC, -PE and -phosphatidylserine (PS) as acyl acceptors. Isozymes 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, suggesting a dual role in glycerolipid synthesis and remodeling. AGPAT2 plays a critical, non-redundant role in adipogenesis related to triglyceride (TG) synthesis and/or provision of phosphatidic acid (PA) for differentiation-dependent signaling pathways Homo sapiens
physiological function while isozymes AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, other isoforms utilize lyso-PC, -PE and -phosphatidylserine (PS) as acyl acceptors. Isozymes 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, suggesting a dual role in glycerolipid synthesis and remodeling. AGPAT2 plays a critical, non-redundant role in adipogenesis related to triglyceride (TG) synthesis and/or provision of phosphatidic acid (PA) for differentiation-dependent signaling pathways Mus musculus
physiological function while isozymes AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, other isoforms utilize lyso-PC, -PE and -phosphatidylserine (PS) as acyl acceptors. Isozymes 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, suggesting a dual role in glycerolipid synthesis and remodeling. AGPAT3 and AGPAT5 can produce PA for nuclear envelope-localized glycerolipid synthesis Homo sapiens
physiological function while isozymes AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, other isoforms utilize lyso-PC, -PE and -phosphatidylserine (PS) as acyl acceptors. Isozymes 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, suggesting a dual role in glycerolipid synthesis and remodeling. Isozyme AGPAT4 has a possible role for incorporating docosahexaenoic acid into brain glycerophospholipids Homo sapiens