Glycerol-3-phosphate acyltransferases: Rate limiting enzymes of triacylglycerol biosynthesis

Four homologous isoforms of glycerol-3-phosphate acyltransferase (GPAT), each the product of a separate gene, catalyze the synthesis of lysophosphatidic acid from glycerol-3-phosphate and long-chain acyl-CoA. This step initiates the synthesis of all the glycerolipids and evidence from gain-of-functi...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2009-06, Vol.1791 (6), p.501-506
Main Authors: Wendel, Angela A., Lewin, Tal M., Coleman, Rosalind A.
Format: Article
Language:English
Subjects:
Acyl Coenzyme A - metabolism
Animals
Diacylglycerol
Fatty Acids - metabolism
Glycerol-3-Phosphate O-Acyltransferase - metabolism
Glycerolipid
Glycerophosphates - metabolism
Humans
Isoenzymes
Kinetics
Lipid droplet
Lipogenesis
Lysophosphatidic acid
Lysophospholipids - metabolism
Membrane
Mice
Microsomes - enzymology
Mitochondrial Membranes - enzymology
Organelles - enzymology
Phospholipid
Triglycerides - biosynthesis
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Summary:Four homologous isoforms of glycerol-3-phosphate acyltransferase (GPAT), each the product of a separate gene, catalyze the synthesis of lysophosphatidic acid from glycerol-3-phosphate and long-chain acyl-CoA. This step initiates the synthesis of all the glycerolipids and evidence from gain-of-function and loss-of-function studies in mice and in cell culture strongly suggests that each isoform contributes to the synthesis of triacylglycerol. Much work remains to fully delineate the regulation of each GPAT isoform and its individual role in triacylglycerol synthesis.
ISSN:1388-1981
0006-3002
1879-2618
DOI:10.1016/j.bbalip.2008.10.010