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

Biochim Biophys Acta. 2009 Jun;1791(6):501-6. doi: 10.1016/j.bbalip.2008.10.010. Epub 2008 Nov 7.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Acyl Coenzyme A / metabolism
  • Animals
  • Fatty Acids / metabolism
  • Glycerol-3-Phosphate O-Acyltransferase / metabolism*
  • Glycerophosphates / metabolism
  • Humans
  • Isoenzymes
  • Kinetics
  • Lipogenesis*
  • Lysophospholipids / metabolism
  • Mice
  • Microsomes / enzymology
  • Mitochondrial Membranes / enzymology
  • Organelles / enzymology
  • Triglycerides / biosynthesis*

Substances

  • Acyl Coenzyme A
  • Fatty Acids
  • Glycerophosphates
  • Isoenzymes
  • Lysophospholipids
  • Triglycerides
  • alpha-glycerophosphoric acid
  • Glycerol-3-Phosphate O-Acyltransferase
  • lysophosphatidic acid