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Literature summary for 2.3.1.15 extracted from

  • Takeuchi, K.; Reue, K.
    Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymes in triglyceride synthesis (2009), Am. J. Physiol. Endocrinol. Metab., 296, E1195-E1209.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information insulin treatment of rat primary adipocytes acutely increases the Km and Vmax of GPAT1 for its substrates, which may be mediated through protein phosphorylation Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Mus musculus 5783
-
endoplasmic reticulum
-
Homo sapiens 5783
-
mitochondrion
-
Mus musculus 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
calculated from cDNA Mus musculus
50000
-
calculated from cDNA Homo sapiens
52000
-
calculated from cDNA Mus musculus
52000
-
calculated from cDNA Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q53EU6
-
-
Homo sapiens Q86UL3
-
-
Mus musculus Q14DK4
-
-
Mus musculus Q61586
-
-
Mus musculus Q8C0N2
-
-
Mus musculus Q8K2C8
-
-
Rattus norvegicus
-
-
-
Rattus norvegicus P97564
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein insulin treatment of rat primary adipocytes acutely increases the Km and Vmax of GPAT1 for its substrates, which may be mediated through protein phosphorylation Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
GPAT1 from rat is purified to homogeneity Rattus norvegicus
GPAT1 from rat is purified to homogeneity Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
3T3-L1 cell Gpat3 mRNA increases 60fold during differentiation of 3T3-L1 preadipocytes to mature adipocytes, suggesting a critical role in adipocytes Mus musculus
-
adipocyte
-
Rattus norvegicus
-
adipose tissue moderate expression Homo sapiens
-
adipose tissue highest expression in white adipose tissue, moderate in brown adipose tissue Mus musculus
-
brain low expression Homo sapiens
-
brain moderate expression Mus musculus
-
brown adipose tissue high expression Mus musculus
-
cerebellum moderate expression Homo sapiens
-
enteric nervous system moderate expression Mus musculus
-
epididymis highest expression Mus musculus
-
heart high expression Homo sapiens
-
heart low expression Mus musculus
-
heart moderate expression Mus musculus
-
HEK-293 cell
-
Homo sapiens
-
intestine moderate expression Mus musculus
-
kidney high expression Homo sapiens
-
kidney moderate expression Mus musculus
-
liver
-
Mus musculus
-
liver low expression Homo sapiens
-
liver moderate expression Mus musculus
-
liver mRNA expression is induced by insulin Mus musculus
-
lung moderate expression Mus musculus
-
lung moderate expression Homo sapiens
-
skeletal muscle high expression Homo sapiens
-
skeletal muscle low expression Mus musculus
-
skeletal muscle moderate expression Mus musculus
-
small intestine highest expression Mus musculus
-
spleen low expression Homo sapiens
-
spleen moderate expression Mus musculus
-
stomach moderate expression Mus musculus
-
testis high expression Homo sapiens
-
testis high expression Mus musculus
-
thyroid high expression Homo sapiens
-
white adipose tissue moderate expression Mus musculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
GPAT2 activity constitutes 60% of GPAT activity in purified mitochondria from wild-type mouse liver Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in biochemical studies, saturated fatty acyl-CoAs are preferred approximately 2fold over unsaturated fatty acyl-CoAs as GPAT1 substrates. Esterification occurs at the sn-1 position of glycerol 3-phosphate Rattus norvegicus ?
-
?

Synonyms

Synonyms Comment Organism
glycerol-3-phosphate acyltransferase 1 four isoenzymes are identified in mammals Rattus norvegicus
glycerol-3-phosphate acyltransferase 1 four isoenzymes are identified in mammals Mus musculus
glycerol-3-phosphate acyltransferase 2 four isoenzymes are identified in mammals Rattus norvegicus
glycerol-3-phosphate acyltransferase 2 four isoenzymes are identified in mammals Mus musculus
glycerol-3-phosphate acyltransferase 3 four isoenzymes are identified in mammals Mus musculus
glycerol-3-phosphate acyltransferase 3 four isoenzymes are identified in mammals Homo sapiens
glycerol-3-phosphate acyltransferase 4 four isoenzymes are identified in mammals Mus musculus
glycerol-3-phosphate acyltransferase 4 four isoenzymes are identified in mammals Homo sapiens
GPAT1
-
Rattus norvegicus
GPAT1
-
Mus musculus
GPAT2
-
Rattus norvegicus
GPAT2
-
Mus musculus
GPAT3
-
Mus musculus
GPAT3
-
Homo sapiens
GPAT4
-
Mus musculus
GPAT4
-
Homo sapiens

General Information

General Information Comment Organism
malfunction GPAT1 -/- mice contain reduced amounts of C16:0 and increased C18:0 and C18:1 in liver phosphatidylcholine and phosphatidylethanolamine. Phosphatidylcholine and phosphatidylethanolamine in Gpat1-/- liver also contain 40% more C20:4 at the sn-2 position, suggesting that esterification at the sn-2 position is influenced by fatty acids at the sn-1 position. GPAT1 overexpression in liver of mice leads to increased incorporation of C16:0 fatty acids into lysophosphatidic acid, diacylglycerol, triacylglycerol Mus musculus
malfunction GPAT1 overexpression in rat primary hepatocytes results in the increased incorporation of exogenous fatty acids into triacylglycerol and phospholipids and reduced rate of beta-oxidation Rattus norvegicus
malfunction GPAT1-deficient mice fed a high-fat/high sucrose diet have reduced hepatic triacylglycerol but increased plasma beta-hydroxybutyrate and liver acylcarnitine levels, suggesting enhanced beta-oxidation. In the high-fat-fed GPAT1-deficient mice, elevated beta-oxidation is associated with increased hepatic acyl-CoA content and activation state of AMP-activated protein kinase. These results suggest that enhanced beta-oxidation represents increased energy flow to fatty acid oxidation caused by a blockage of the glycerolipid synthesis pathway. In GPAT1-overexpressing mice, liver fatty acid oxidation measured ex vivo is decreased. Due to the enhanced beta-oxidation in Gpat1-/- mice, liver mitochondria exhibit a greater mitochondrial dysfunction (oxidative stress, increased hepatocyte apoptosis, lower level odf DNA repair genes) Mus musculus
malfunction GPAT3 overexpression in human embryonic kidney (HEK)-293 cells leads to increased incorporation of exogenous oleic acid into triacylglycerol but not into phospholipids. GPAT3 overexpression in HEK-293 cells increases phosphorylation of p70 S6 kinase and 4E-binding protein 1 in an mTOR (mammalian target of rapamycin)-dependent manner, suggesting the possible involvement of lipid intermediates of TAG synthesis, such as lysophosphatidic acid and phosphatidic acid (PA), in the mTOR pathway Homo sapiens
malfunction Gpat4-/- mice have severely impaired lactation, a reduced size and number of alveoli, reduced numbers of fat droplets in mammary gland, and reduced triacylglycerol and diacylglycerol content in milk. Gonadal white adipose tissue mass and plasma leptin levels are reduced in Gpat4-/- mice, and subdermal adipose tissue, is nearly absent. The reduced body weight of Gpat4-/- mice is associated with increased energy expenditure Mus musculus
malfunction in GPAT1-overexpressing rats, hepatic acyl-CoA content and plasma beta-hydroxybutyrate concentration are similar to those of control rats Rattus norvegicus
physiological function a 60% knockdown of Gpat3 mRNA in 3T3-L1 cells with small interfering (si)RNA results in a 55% decrease in fatty acid incorporation into lysophosphatidic acid. Gpat1 mRNA levels also show a large induction during 3T3-L1 adipocyte differentiation, suggesting that this isoform also contributes to GPAT activity in adipocytes Mus musculus
physiological function Gpat1 mRNA levels increase more than 20fold in mouse liver in an insulin-dependent manner by refeeding of a high-carbohydrate diet after fasting, which is associated with active hepatic lipogenesis Mus musculus
physiological function Gpat3 mRNA levels in ob/ob mice are decreased by 70% in white adipose tissue and increased 2fold in liver compared with wild-type animals. Treatment of ob/ob mice with rosiglitazone, a potent peroxisome proliferator-activated receptor (PPAR)gamma agonist, increases Gpat3, but not Gpat1, mRNA in white adipose tissue, suggesting that Gpat3 is a PPARgamma target gene Mus musculus
physiological function in contrast to Gpat1, Gpat2 mRNA does not increase in liver of rats refed a high-sucrose diet after fasting, suggesting less contribution of GPAT2 to diet-induced hepatic TAG synthesis Rattus norvegicus
physiological function in contrast to other GPATs, GPAT4 overexpression does not increase incorporation of exogenous fatty acids into triacylglycerol in HEK-293 and COS-7 cells, suggesting that lysophosphatidic acid and phosphatidic acid produced from the GPAT4 pathway may consist of a separate pool from that utilized for triacylglycerol synthesis Homo sapiens
physiological function the mouse Gpat1 gene promoter region contains three sterol regulatory elements responsible for SREBP-1-mediated transactivation. Ectopic expression of SREBP-1c in 3T3-L1 adipocytes or in liver of transgenic mice dramatically increases Gpat1 mRNA Mus musculus