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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum | - |
Mus musculus | 5783 | - |
endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
mitochondrion | - |
Mus musculus | 5739 | - |
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 | 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 | 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 (Comment) | Organism |
---|---|
GPAT1 from rat is purified to homogeneity | Rattus norvegicus |
GPAT1 from rat is purified to homogeneity | Mus musculus |
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 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 | 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 | 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 | 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 |