Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymes

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Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymesin triglyceride synthesis
From  Kazuharu Takeuchi and Karen Reue
Biochemistry, physiology, and genetics of GPAT, AGPAT, and
lipin enzymes in triglyceride synthesis.AmJ Physiol Endocrinol Metab 296: E1195–E1209,
2009. First published March 31, 2009; doi:10.1152/ajpendo.90958.2008.—Triacylglycerol
(TAG) synthesis and storage in tissues such as adipose tissue and liver have
important roles in metabolic homeostasis. The molecular identification of genes
encoding enzymes that catalyze steps in TAG biosynthesis from glycerol 3-phosphate
has revealed an unexpected number of protein isoforms of the glycerol
phosphate acyltransferase (GPAT), acylglycerolphosphate acyltransferase
(AGPAT), and lipin (phosphatidate phosphatase) families that appear to catalyze
similar biochemical reactions. However, on the basis of available data for a few
members in which genetic deficiencies in mouse and/or human have been studied,
we postulate that each GPAT, AGPAT, and lipin family member likely has a
specialized role that may be uncovered through careful biochemical and physiological
analyses.