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evolution
KX256278
PrLPAAT1 may be a member of AGPAT family, and may have acyltransferase activity, comparisons of sequences, genetic structures, and conserved structure motifs, overview. Phylogenetic analysis
evolution
KX256279
the enzyme belongs to the acyl-CoA:1-acylglycerol-sn-3-phosphate acyltranferases (AGPAT) family, PrLPAAT4 possesses a 1-acyl-sn-glycerol-3-phosphate acyltransferase-related domain, it is subordinated to cluster III. Comparative analysis of gene structure and conserved domain in the LPAAT4 proteins
evolution
the LPAAT/PlsC enzymes belong to the evolutionarily conserved lysophospholipid acyltransferase (AGPAT) family of intrinsic membrane proteins. TmPlsC comprises two domains: residues 1-61 create a distinctive N-terminal two-helix motif, and the C-terminal residues 62-247 form an alphabeta domain comprising a seven stranded beta-sheet core surrounded by five alpha-helices and four 310 helices. All four conserved motifs within the AGPAT family are within the alphabeta domain. The N-terminal two-helix motif comprises an anti-parallel two-helix bundle (alpga1 and alpha2), structure comparisons, e.g. with soluble plant GPATs (EC 2.3.1.15), overview
evolution
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the LPAAT/PlsC enzymes belong to the evolutionarily conserved lysophospholipid acyltransferase (AGPAT) family of intrinsic membrane proteins. TmPlsC comprises two domains: residues 1-61 create a distinctive N-terminal two-helix motif, and the C-terminal residues 62-247 form an alphabeta domain comprising a seven stranded beta-sheet core surrounded by five alpha-helices and four 310 helices. All four conserved motifs within the AGPAT family are within the alphabeta domain. The N-terminal two-helix motif comprises an anti-parallel two-helix bundle (alpga1 and alpha2), structure comparisons, e.g. with soluble plant GPATs (EC 2.3.1.15), overview
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evolution
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the LPAAT/PlsC enzymes belong to the evolutionarily conserved lysophospholipid acyltransferase (AGPAT) family of intrinsic membrane proteins. TmPlsC comprises two domains: residues 1-61 create a distinctive N-terminal two-helix motif, and the C-terminal residues 62-247 form an alphabeta domain comprising a seven stranded beta-sheet core surrounded by five alpha-helices and four 310 helices. All four conserved motifs within the AGPAT family are within the alphabeta domain. The N-terminal two-helix motif comprises an anti-parallel two-helix bundle (alpga1 and alpha2), structure comparisons, e.g. with soluble plant GPATs (EC 2.3.1.15), overview
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evolution
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the LPAAT/PlsC enzymes belong to the evolutionarily conserved lysophospholipid acyltransferase (AGPAT) family of intrinsic membrane proteins. TmPlsC comprises two domains: residues 1-61 create a distinctive N-terminal two-helix motif, and the C-terminal residues 62-247 form an alphabeta domain comprising a seven stranded beta-sheet core surrounded by five alpha-helices and four 310 helices. All four conserved motifs within the AGPAT family are within the alphabeta domain. The N-terminal two-helix motif comprises an anti-parallel two-helix bundle (alpga1 and alpha2), structure comparisons, e.g. with soluble plant GPATs (EC 2.3.1.15), overview
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malfunction
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mutations in human CGI-58/ABHD5 cause Chanarin-Dorfman syndrome, characterized by excessive storage of triacylglycerol in tissues
malfunction
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enzyme knockdown inhibits proliferation and anchorage-independent growth of pancreatic cancer cells
malfunction
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striking decreases in both the oxygen consumption rate and the extracellular acidification rate are observed in enzyme-deficient CD4+ T cells following CD3/CD28 stimulation indicating an inherent cellular defect in energy production. In addition, the spare respiratory capacity and the mitochondrial membrane potential of these CD4+T cells is significantly decreased
malfunction
deletion of the SlPlsC1 gene causes a marked decrease in the amounts of eicosapentaenoic acid (EPA)-containing phospholipids, without significantly altering the composition of other phospholipids. The EPA-containing phospholipids play an important role in survival of the bacterium in a cold environment
malfunction
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enzyme-deficient mice develop widespread disturbances of metabolism, sperm development, and neurologic function resulting from disrupted phospholipid homeostasis. Enzyme-deficient mice have reduced body weight, total body fat, and plasma leptin level and show features of epilepsy. Neonatal enzyme-deficient mice have minor alterations in lipid synthesis and reduced plasma glucose levels. Enzyme-deficient males and females mice have reproductive abnormalities
malfunction
in a plsC4-disrupted mutant, phospholipids (PLs) containing 13:0 found in the parental strain are almost completely absent. The loss of these PLs is suppressed by introduction of a plsC4-expression plasmid. PLs containing 15:0 are also drastically decreased by plsC4 disruption
malfunction
in cultured adipocytes, knockdown of AGPAT2 reduces TG synthesis and increased lyso-PA channeling into phospholipids
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
malfunction
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deletion of the SlPlsC1 gene causes a marked decrease in the amounts of eicosapentaenoic acid (EPA)-containing phospholipids, without significantly altering the composition of other phospholipids. The EPA-containing phospholipids play an important role in survival of the bacterium in a cold environment
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malfunction
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in a plsC4-disrupted mutant, phospholipids (PLs) containing 13:0 found in the parental strain are almost completely absent. The loss of these PLs is suppressed by introduction of a plsC4-expression plasmid. PLs containing 15:0 are also drastically decreased by plsC4 disruption
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metabolism
LPAAT is a key intermediate in the biosynthesis of membrane phospholipids in all tissues and storage lipids in developing seeds
metabolism
C4B4E7
the enzyme provides an an alternative important possibility to produce phosphatidylinositol in the testis
metabolism
the enzyme specifically supports synthesis of brain phosphatidylinositol, phosphatidylcholine, and phosphatidylethanolamine
metabolism
phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis
metabolism
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plsC plays an important role in tigecycline resistance. Tigecycline resistance in Acinetobacter baumannii is mediated by frameshift mutation in plsC. Change in the cellular membrane caused by plsC mutation is detected by flow cytometry. It is concluded that cellular membrane change may play an important role in tigecycline resistance in Acinetobacter baumannii
metabolism
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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)
metabolism
phosphatidic acid is the central intermediate in membrane phospholipid synthesis and is generated by two acyltransferases in a pathway conserved in all life forms. The second step in this pathway is catalyzed by 1-acyl-sn-glycero-3-phosphate acyltransferase, called PlsC in bacteria
metabolism
KX256279
PrLPAAT4 plays an important role in seed fatty acid biosynthesis
metabolism
the enzyme is involved in the biosynthesis of glycerolipids in Cyanothece sp. PCC 8801, overview
metabolism
the plastidial lysophosphatidic acid acyltransferase of the unicellular green alga Chlamydomonas reinhardtii (CrLPAAT1) is a key enzyme in triacylglycerol biosynthesis. In microalgae, de novo biosynthesis of triacylglycerol (TAG) via the Kennedy pathway involves successive acylation of glycerol-3-phosphate (G-3-P) by glycerol-3-phosphate acyltransferase (GPAT, EC 2.3.1.15), lysophosphatidic acid acyltransferase (LPAAT, EC 2.3.1.51), and diacylglycerol acyltransferase (DGAT, EC 2.3.1.20). Analysis of the affinity between CrLPAAT1 and CrGPATcl, binding kinetics. The strength of CrLPAAT1-CrGPATcl interaction varied with the pH values, which peaks in the neutral environment and is gradually diminished in both acidic and alkaline buffers. CrLPAAT1-CrGPATcl tend to be dissociated with the increased concentration of C18:1(n9)-LPA, whereas G-3-P has no effect on the interaction between these two proteins. Besides, the stability of CrLPAAT1-CrGPATcl complex is inversely proportional to the concentrations of acyl donors used in the assays, and it is found to be the most sensitive to the high-concentration of C18:1(n9)-CoA among various acyl donors
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
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
metabolism
KX256278
through the conventional Kennedy pathway in the endoplasmic reticulum, triacylglycerol (TAG) is synthesized de novo in three acylation reactions at the sn-1-, sn-2-, and sn-3-positions of the glycerol-3-phosphate backbone with acyl chains from acyl-CoAs, and these three reactions respectively are catalyzed by glycerol-3-phosphate acyltransferase (GPAT, EC 2.3.1.15), LPAAT, and diacylglycerol acyltransferase (DGAT, EC 2.3.1.20)
metabolism
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phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis
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metabolism
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the enzyme provides an an alternative important possibility to produce phosphatidylinositol in the testis
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metabolism
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phosphatidic acid is the central intermediate in membrane phospholipid synthesis and is generated by two acyltransferases in a pathway conserved in all life forms. The second step in this pathway is catalyzed by 1-acyl-sn-glycero-3-phosphate acyltransferase, called PlsC in bacteria
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metabolism
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phosphatidic acid is the central intermediate in membrane phospholipid synthesis and is generated by two acyltransferases in a pathway conserved in all life forms. The second step in this pathway is catalyzed by 1-acyl-sn-glycero-3-phosphate acyltransferase, called PlsC in bacteria
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metabolism
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phosphatidic acid is the central intermediate in membrane phospholipid synthesis and is generated by two acyltransferases in a pathway conserved in all life forms. The second step in this pathway is catalyzed by 1-acyl-sn-glycero-3-phosphate acyltransferase, called PlsC in bacteria
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physiological function
LPAAT is a crucial enzyme controlling the metabolic flow of lysophosphatidic acid into the pool of phosphatidic acid, which plays a key role in many physiological aspects, such as cell signaling, cell polarity, and apoptotic signaling cascades in higher eukaryotes. Phosphatidic acid specifically regulates the genes involved in modulating cell shape and organization
physiological function
LPAAT plays an essential role in the synthesis of phosphatidic acid
physiological function
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LPAAT3 regulates Golgi complex structure and function, overview
physiological function
expression of isoform CGI-58 in fibroblasts from humans with Chanarin-Dorfman increases the incorporation of fatty acids released from the lipolysis of stored triacylglycerols into phospholipids
physiological function
expression of isoform LPAATbeta is readily detected in 8 of 10 analyzed human osteosarcoma lines. Exogenous expression of LPAATbeta promotes osteosarcoma cell proliferation and migration, while silencing LPAATbeta expression inhibits these cellular characteristics.Exogenous expression of LPAATbeta effectively promotes tumor growth, while knockdown of LPAATbeta expression inhibits tumor growth in an orthotopic xenograft model of human osteosarcoma
physiological function
isoform AGPAT1 is involved in development of skeletal muscle. Small interference RNA-mediated knockdown of AGPAT1 expression prevents the induction of myogenin, and inhibits the expression of myosin heavy chain. This effect is rescued by transfection with AGPAT1 but not AGPAT2. The regulation of myogenesis by AGPAT1 is associated with alterations on actin cytoskeleton. AGPAT1 colocalizes AGPAT1 to areas of active actin polymerization. AGPAT1 overexpression is not associated with an increase in phosphatidic acid levels
physiological function
C4B4E7
isoform LPAAT3 is induced during germ cell maturation. Differentiation of mouse GC-2spd(ts) spermatocytes into spermatides up-regulates isoform LPAAT3 mRNA, increases the amount of polyunsaturated phospholipids, and shifts the specificity for the incorporation of docosahexaenoic acid toward phosphatidylcholine and phosphatidylethanolamine. Stable knockdown of LPAAT3 in GC-2spd(ts) cells significantly decreases microsomal LPAAT3 activity, reduces levels of polyunsaturated phosphatidylethanolamine species, and impairs cell proliferation/survival during geneticin selection
physiological function
C4B4E7
stable transfection of TM4 Sertoli cells with isoform LPAAT3-small hairpin RNA leads to decreases in arachidonoyl-, eicosapentaenoyl-, and docosapentaenoyl-containing phosphatidylcholine and linoleoyl-containing phosphatidylethanolamine, phosphatidylserine, and phosphatidylglycerol. Expression of murine LPAAT3 in Chinese hamster ovary K1 cells has essentially an opposite effect. The level of polyunsaturated phosphatidylcholine correlates with cellular levels of free docosapentaenoic acid and eicosapentaenoic acid in TM4 and Chinese hamster ovary K1 cells, respectively
physiological function
strains deficient for the enzyme show abnormalities in lipid droplet morphology and contain more lipid droplets, while overexpression results in fewer lipid droplets. Mutant strains reveal a significant reduction in triacylglycerol content, while phospholipid composition remains unchanged. Both phopholipids and glycerolipids are qualitatively affected by the mutation
physiological function
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the enzyme is essential for the response to the increased metabolic demands associated with T cell activation
physiological function
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the enzyme regulates mTOR signaling by affecting its association with FKBP38 and regulates nuclear shape and Lipin 1 nuclear localization
physiological function
enzyme PlsC dictates the acyl chain composition of the 2-position of phospholipids, and the acyl chain selectivity ruler is an appropriately placed and closed hydrophobic tunnel
physiological function
expression of MaLPAAT in transgenic Yarrowia lipolytica results in higher accumulation of EPA (20:5omega3) and docosahexaenoic acid (DHA) in total fatty acid
physiological function
KX256279
lysophosphatidic acid acyltransferases (LPAATs) are essential for the acylation of lysophosphatidic acid (LPA) and the synthesis of phosphatidic acid (PA), a key intermediate in the synthesis of membrane phospholipids and storage lipids. PrLPAAT4, a putative lysophosphatidic acid acyltransferase from Paeonia rockii, plays an important role in seed fatty acid biosynthesis. LPAATs play a crucial role in catalyzing the second step of triacylglycerol (TAG) formation, determining TAGs acyl composition at the sn-2-position, and controlling the conversion of LPA to PA. PrLPAAT4 might function as a positive regulator in seed fatty acid biosynthesis
physiological function
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Mortierella alpina is a fungus producing a high level of arachidonic acid (20:4, omega6)
physiological function
KX256278
PrLPAAT1 is an important component in the fatty acid accumulation process, especially during the early stages of seed development. 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
physiological function
the 1-acyl-sn-glycerol-3-phosphate O-acyltransferase homologue is responsible for the synthesis of membrane phospholipids with a branched-chain fatty acyl group in Shewanella livingstonensis Ac10. 1-Acyl-sn-glycerol-3-phosphate O-acyltransferase (PlsC) plays an essential role in the formation of phosphatidic acid, a precursor of various membrane phospholipids (PLs), in bacteria by catalyzing the introduction of an acyl group into the sn-2 position of lysophosphatidic acid. Isozyme PlsC4 is a distinct type of PlsC homologue that is responsible for the synthesis of PLs containing a branched-chain fatty acyl group at the sn-2 position and plays a clearly different role from that of PlsC1 in vivo. Gas chromatography-mass spectrometry analysis of fatty acyl methyl esters derived from PLs of the PlsC4 parental strain shows that the 13:0 and 15:0 groups are an 11-methyllauroyl group and a 13-methylmyristoyl group, respectively. Phospholipase A2 treatment reveals that these fatty acyl groups are linked to the sn-2 position of PLs
physiological function
the bacterium produces glycerophospholipids that are esterified at the sn-2 position with a polyunsaturated fatty acid, namely eicosapentaenoic acid (EPA), via 1-acyl-sn-glycerol-3-phosphate acyltransferase PlsC. Isozyme SlPlsC1, one of five, appears to be dedicated for the in vivo acylation of lysophosphatidic acid (LPA) with EPA. SlPlsC1 is dedicated to the production of phosphatidic acid and is not involved in the acyl chain remodeling of phospholipids with a head group. SlPlsC1 can utilize a broad range of unsaturated fatty acyl-CoAs in vitro. A possible explanation for this seeming discrepancy may be that four other PlsC homologs (SlPlsC2, SlPlsC3, SlPlsC4 and SlPlsC5) present in Shewanella livingstonensis strain Ac10 can compensate for the lack of SlPlsC1 except for the acylation
physiological function
the enzyme is involved in the formation of the membrane of the human pathogen Chlamydia trachomatis. 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. Both the bacterial acyltransferase CT775 and human host LPCAT1 can transfer branched acyl-CoA to 1-acyl-GPC to form PC, thereby providing evidence for the presence of a system in which host lipids are modified by the addition of bacterial branched fatty acid within the inclusion
physiological function
the high content of 14:0 in Cyanothece sp. PCC 8801 might be a result of the high specificity of the 1-acyl-sn-glycerol-3-phosphate acyltransferase activity toward the 14:0-acyl-carrier protein. The 14:0 fatty acid is esterified primarily to the sn-2 position of the glycerol moiety of glycerolipids. This characteristic is unique because, in most of the cyanobacterial strains, the sn-2 position is esterified exclusively with C16 fatty acids, generally 16:0. The enzyme from Cyanothece sp. PCC 8801 transfers an acyl group from acyl-acyl-carrier protein (acyl-ACP) to lysophosphatidic acid (LPA) for the synthesis of phosphatidic acid (PA), a precursor of glycerolipids. Fatty acid analysis of total glycerolipids in Cyanothece sp. PCC 8801 reveals that myristic acid (14:0) and linoleic acid [18:2(9,12)] are the two major fatty acids, with minor contributions from palmitic acid (16:0), palmitoleic acid [16:1(9)], stearic acid (18:0), and oleic acid [18:1(9)], overview
physiological function
the plastidial lysophosphatidic acid acyltransferase of the unicellular green alga Chlamydomonas reinhardtii (CrLPAAT1) is a key enzyme involved in triacylglycerol biosynthesis
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
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
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
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
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
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
physiological function
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the bacterium produces glycerophospholipids that are esterified at the sn-2 position with a polyunsaturated fatty acid, namely eicosapentaenoic acid (EPA), via 1-acyl-sn-glycerol-3-phosphate acyltransferase PlsC. Isozyme SlPlsC1, one of five, appears to be dedicated for the in vivo acylation of lysophosphatidic acid (LPA) with EPA. SlPlsC1 is dedicated to the production of phosphatidic acid and is not involved in the acyl chain remodeling of phospholipids with a head group. SlPlsC1 can utilize a broad range of unsaturated fatty acyl-CoAs in vitro. A possible explanation for this seeming discrepancy may be that four other PlsC homologs (SlPlsC2, SlPlsC3, SlPlsC4 and SlPlsC5) present in Shewanella livingstonensis strain Ac10 can compensate for the lack of SlPlsC1 except for the acylation
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physiological function
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the 1-acyl-sn-glycerol-3-phosphate O-acyltransferase homologue is responsible for the synthesis of membrane phospholipids with a branched-chain fatty acyl group in Shewanella livingstonensis Ac10. 1-Acyl-sn-glycerol-3-phosphate O-acyltransferase (PlsC) plays an essential role in the formation of phosphatidic acid, a precursor of various membrane phospholipids (PLs), in bacteria by catalyzing the introduction of an acyl group into the sn-2 position of lysophosphatidic acid. Isozyme PlsC4 is a distinct type of PlsC homologue that is responsible for the synthesis of PLs containing a branched-chain fatty acyl group at the sn-2 position and plays a clearly different role from that of PlsC1 in vivo. Gas chromatography-mass spectrometry analysis of fatty acyl methyl esters derived from PLs of the PlsC4 parental strain shows that the 13:0 and 15:0 groups are an 11-methyllauroyl group and a 13-methylmyristoyl group, respectively. Phospholipase A2 treatment reveals that these fatty acyl groups are linked to the sn-2 position of PLs
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physiological function
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the enzyme is involved in the formation of the membrane of the human pathogen Chlamydia trachomatis. 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. Both the bacterial acyltransferase CT775 and human host LPCAT1 can transfer branched acyl-CoA to 1-acyl-GPC to form PC, thereby providing evidence for the presence of a system in which host lipids are modified by the addition of bacterial branched fatty acid within the inclusion
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physiological function
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enzyme PlsC dictates the acyl chain composition of the 2-position of phospholipids, and the acyl chain selectivity ruler is an appropriately placed and closed hydrophobic tunnel
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physiological function
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enzyme PlsC dictates the acyl chain composition of the 2-position of phospholipids, and the acyl chain selectivity ruler is an appropriately placed and closed hydrophobic tunnel
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physiological function
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enzyme PlsC dictates the acyl chain composition of the 2-position of phospholipids, and the acyl chain selectivity ruler is an appropriately placed and closed hydrophobic tunnel
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additional information
a two-helix motif positions the active site of lysophosphatidic acid acyltransferase is required for catalysis within the membrane bilayer. The structure of PlsC shows an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase alphabeta domain that contains the catalytic HX4D motif. Molecular dynamics simulations reveal that the two-helix motif represents a substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer using soluble acyl donors. Catalytic mechanism and substrate binding sites, overview
additional information
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a two-helix motif positions the active site of lysophosphatidic acid acyltransferase is required for catalysis within the membrane bilayer. The structure of PlsC shows an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase alphabeta domain that contains the catalytic HX4D motif. Molecular dynamics simulations reveal that the two-helix motif represents a substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer using soluble acyl donors. Catalytic mechanism and substrate binding sites, overview
additional information
KX256279
comparative structure deduction and analysis of PrLPAAT4
additional information
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comparative structure deduction and analysis of PrLPAAT4
additional information
KX256278
PrLPAAT1 structure prediction and modelling, overview
additional information
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PrLPAAT1 structure prediction and modelling, overview
additional information
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a two-helix motif positions the active site of lysophosphatidic acid acyltransferase is required for catalysis within the membrane bilayer. The structure of PlsC shows an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase alphabeta domain that contains the catalytic HX4D motif. Molecular dynamics simulations reveal that the two-helix motif represents a substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer using soluble acyl donors. Catalytic mechanism and substrate binding sites, overview
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additional information
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a two-helix motif positions the active site of lysophosphatidic acid acyltransferase is required for catalysis within the membrane bilayer. The structure of PlsC shows an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase alphabeta domain that contains the catalytic HX4D motif. Molecular dynamics simulations reveal that the two-helix motif represents a substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer using soluble acyl donors. Catalytic mechanism and substrate binding sites, overview
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additional information
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a two-helix motif positions the active site of lysophosphatidic acid acyltransferase is required for catalysis within the membrane bilayer. The structure of PlsC shows an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase alphabeta domain that contains the catalytic HX4D motif. Molecular dynamics simulations reveal that the two-helix motif represents a substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer using soluble acyl donors. Catalytic mechanism and substrate binding sites, overview
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