Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and plants: A novel enzyme in phosphatidylcholine synthesis

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Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and plants : A novel enzyme in phosphatidylcholine synthesis. / Głab, Bartosz; Beganovic, Mirela; Anaokar, Sanket; Hao, Mengshu; Rasmusson, Allan G.; Patton-Vogt, Jana; Banaś, Antoni; Stymne, Sten; Lager, Ida.

In: Journal of Biological Chemistry, Vol. 291, No. 48, 25.11.2016, p. 25066-25076.

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Głab, Bartosz ; Beganovic, Mirela ; Anaokar, Sanket ; Hao, Mengshu ; Rasmusson, Allan G. ; Patton-Vogt, Jana ; Banaś, Antoni ; Stymne, Sten ; Lager, Ida. / Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and plants : A novel enzyme in phosphatidylcholine synthesis. In: Journal of Biological Chemistry. 2016 ; Vol. 291, No. 48. pp. 25066-25076.

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TY - JOUR

T1 - Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and plants

T2 - A novel enzyme in phosphatidylcholine synthesis

AU - Głab, Bartosz

AU - Beganovic, Mirela

AU - Anaokar, Sanket

AU - Hao, Mengshu

AU - Rasmusson, Allan G.

AU - Patton-Vogt, Jana

AU - Banaś, Antoni

AU - Stymne, Sten

AU - Lager, Ida

PY - 2016/11/25

Y1 - 2016/11/25

N2 - Glycero-3-phosphocholine (GPC), the product of the complete deacylation of phosphatidylcholine (PC), was long thought to not be a substrate for reacylation. However, it was recently shown that cell-free extracts from yeast and plants could acylate GPC with acyl groups from acyl-CoA. By screening enzyme activities of extracts derived from a yeast knock-out collection, we were able to identify and clone the yeast gene (GPC1) encoding the enzyme, named glycerophosphocholine acyltransferase (GPCAT). By homology search, we also identified and cloned GPCAT genes from three plant species. All enzymes utilize acyl-CoA to acylate GPC, forming lyso-PC, and they show broad acyl specificities in both yeast and plants. In addition to acyl-CoA, GPCAT efficiently utilizes LPC and lysophosphatidylethanolamine as acyl donors in the acylation of GPC. GPCAT homologues were found in the major eukaryotic organism groups but not in prokaryotes or chordates. The enzyme forms its own protein family and does not contain any of the acyl binding or lipase motifs that are present in other studied acyltransferases and transacylases. In vivo labeling studies confirm a role for Gpc1p in PC biosynthesis in yeast. It is postulated that GPCATs contribute to the maintenance of PC homeostasis and also have specific functions in acyl editing of PC (e.g. in transferring acyl groups modified at the sn-2 position of PC to the sn-1 position of this molecule in plant cells).

AB - Glycero-3-phosphocholine (GPC), the product of the complete deacylation of phosphatidylcholine (PC), was long thought to not be a substrate for reacylation. However, it was recently shown that cell-free extracts from yeast and plants could acylate GPC with acyl groups from acyl-CoA. By screening enzyme activities of extracts derived from a yeast knock-out collection, we were able to identify and clone the yeast gene (GPC1) encoding the enzyme, named glycerophosphocholine acyltransferase (GPCAT). By homology search, we also identified and cloned GPCAT genes from three plant species. All enzymes utilize acyl-CoA to acylate GPC, forming lyso-PC, and they show broad acyl specificities in both yeast and plants. In addition to acyl-CoA, GPCAT efficiently utilizes LPC and lysophosphatidylethanolamine as acyl donors in the acylation of GPC. GPCAT homologues were found in the major eukaryotic organism groups but not in prokaryotes or chordates. The enzyme forms its own protein family and does not contain any of the acyl binding or lipase motifs that are present in other studied acyltransferases and transacylases. In vivo labeling studies confirm a role for Gpc1p in PC biosynthesis in yeast. It is postulated that GPCATs contribute to the maintenance of PC homeostasis and also have specific functions in acyl editing of PC (e.g. in transferring acyl groups modified at the sn-2 position of PC to the sn-1 position of this molecule in plant cells).

UR - http://www.scopus.com/inward/record.url?scp=84997606226&partnerID=8YFLogxK

U2 - 10.1074/jbc.M116.743062

DO - 10.1074/jbc.M116.743062

M3 - Article

C2 - 27758859

AN - SCOPUS:84997606226

VL - 291

SP - 25066

EP - 25076

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 1083-351X

IS - 48

ER -