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Review
. 2011 Nov;6(11):1695-9.
doi: 10.4161/psb.6.11.17777. Epub 2011 Nov 1.

sn-Glycerol-3-phosphate acyltransferases in plants

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Review

sn-Glycerol-3-phosphate acyltransferases in plants

Xue Chen et al. Plant Signal Behav. 2011 Nov.

Abstract

sn-Glycerol-3-phosphate acyltransferase (GPAT) catalyzes the acylation at sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid (LPA). LPA is an important intermediate for the formation of different types of acyl-lipids, such as extracellular lipid polyesters, storage and membrane lipids. Three types of GPAT have been found in plants, localizing to the plastid, endoplasmic reticulum, and mitochondria. These GPATs are involved in several lipid biosynthetic pathways and play important biological roles in plant development. In the present review, we will focus on the recent progress in studying the physiological functions of GPATs and their metabolic roles in glycerolipid biosynthesis.

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Figures

Figure 1.
Figure 1.
The GPAT-catalyzed reaction. GPAT catalyzes the esterification of a fatty acyl moiety from acyl-CoA or acly-ACP to the sn-1 position of G3P to form LPA. ACP, acyl carrier protein; CoA, coenzyme A; G3P, sn-glycerol-3-phosphate; GPAT, sn-glycerol-3-phosphate acyltransferase; LPA, lysophosphatidate.
Figure 2.
Figure 2.
Phylogenetic analysis of the GPATs from Arabidopsis (At), Homo sapiens (Hs) and Saccharomyces cerevisiae (Sc). Arabidopsis GPAT1–8 (AtGPAT1–8) evolved quite distantly from the human GPATs (HsGPAT1–4) and yeast GPATs (ScGPAT1–2). Unlike other AtGPATs, the putative AtGPAT9 exhibits a closer evolutionary relationship with the human ER membrane-bound GPAT (HsGPAT3–4). AtGPAT1–3 and HsGPAT1–2 are mitochondrial membrane-bound proteins. AtGPAT4–9, HsGPAT3–4 and ScGPAT1–2 are ER membrane-bound proteins. ATS1 is a soluble GPAT protein located in the plastid stroma of Arabidopsis. The GPAT amino acid sequences were subjected to phylogenetic analysis using the PHYML program of the Geneious software.

References

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