Acyl-CoA lysophosphatidylcholine acyltransferases (LPCATs) of Camelina sativa seeds: biochemical properties and function

The transfer of polyunsaturated fatty acids from the location of their synthesis (phosphatidylcholine) to other lipids, e.g., triacylglycerol, remains insufficiently understood. Several enzymes could be involved in this process. One of these enzymes is acyl-CoA:lysophosphatidylcholine acyltransferas...

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Published inPlanta Vol. 250; no. 5; pp. 1655 - 1670
Main Authors Klińska, Sylwia, Jasieniecka-Gazarkiewicz, Katarzyna, Banaś, Antoni
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer Science + Business Media 01.11.2019
Springer Berlin Heidelberg
Springer Nature B.V
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Abstract The transfer of polyunsaturated fatty acids from the location of their synthesis (phosphatidylcholine) to other lipids, e.g., triacylglycerol, remains insufficiently understood. Several enzymes could be involved in this process. One of these enzymes is acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs). In Camelina sativa seeds, LPCATs could be one of the most important players in this process. Our data clearly indicate that the CsLPCATs present in developing seeds have the potential to transfer almost all polyunsaturated fatty acids synthesised on phosphatidylcholine to the acyl-CoA pool. CsLPCAT activity is the highest at 30°C, and the enzymes operate well at a pH of 7.0–11.0, with the best activity at a pH of 9.0. The activity of CsLPCATs was inhibited by calcium and magnesium ions at a concentration of 0.05–2 mM. In the forward reaction, CsLPCATs preferentially utilise 18:2-CoA; however, other C18 unsaturated fatty acids are also well accepted. In the backward reactions, there is no clear discrimination between the C18 unsaturated fatty acids utilised by the enzymes for phosphatidylcholine remodelling. The activity of CsLPCATs does not differ much between the stages of seed development.
AbstractList The transfer of polyunsaturated fatty acids from phosphatidylcholine to other lipids involves several enzymes. In Camelina sativa seeds, acyl-CoA:lysophosphatidylcholine acyltransferases could be one of the most important players in this process. The transfer of polyunsaturated fatty acids from the location of their synthesis (phosphatidylcholine) to other lipids, e.g., triacylglycerol, remains insufficiently understood. Several enzymes could be involved in this process. One of these enzymes is acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs). In Camelina sativa seeds, LPCATs could be one of the most important players in this process. Our data clearly indicate that the CsLPCATs present in developing seeds have the potential to transfer almost all polyunsaturated fatty acids synthesised on phosphatidylcholine to the acyl-CoA pool. CsLPCAT activity is the highest at 30 °C, and the enzymes operate well at a pH of 7.0-11.0, with the best activity at a pH of 9.0. The activity of CsLPCATs was inhibited by calcium and magnesium ions at a concentration of 0.05-2 mM. In the forward reaction, CsLPCATs preferentially utilise 18:2-CoA; however, other C18 unsaturated fatty acids are also well accepted. In the backward reactions, there is no clear discrimination between the C18 unsaturated fatty acids utilised by the enzymes for phosphatidylcholine remodelling. The activity of CsLPCATs does not differ much between the stages of seed development.
MAIN CONCLUSIONThe transfer of polyunsaturated fatty acids from phosphatidylcholine to other lipids involves several enzymes. In Camelina sativa seeds, acyl-CoA:lysophosphatidylcholine acyltransferases could be one of the most important players in this process. The transfer of polyunsaturated fatty acids from the location of their synthesis (phosphatidylcholine) to other lipids, e.g., triacylglycerol, remains insufficiently understood. Several enzymes could be involved in this process. One of these enzymes is acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs). In Camelina sativa seeds, LPCATs could be one of the most important players in this process. Our data clearly indicate that the CsLPCATs present in developing seeds have the potential to transfer almost all polyunsaturated fatty acids synthesised on phosphatidylcholine to the acyl-CoA pool. CsLPCAT activity is the highest at 30 °C, and the enzymes operate well at a pH of 7.0-11.0, with the best activity at a pH of 9.0. The activity of CsLPCATs was inhibited by calcium and magnesium ions at a concentration of 0.05-2 mM. In the forward reaction, CsLPCATs preferentially utilise 18:2-CoA; however, other C18 unsaturated fatty acids are also well accepted. In the backward reactions, there is no clear discrimination between the C18 unsaturated fatty acids utilised by the enzymes for phosphatidylcholine remodelling. The activity of CsLPCATs does not differ much between the stages of seed development.
The transfer of polyunsaturated fatty acids from the location of their synthesis (phosphatidylcholine) to other lipids, e.g., triacylglycerol, remains insufficiently understood. Several enzymes could be involved in this process. One of these enzymes is acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs). In Camelina sativa seeds, LPCATs could be one of the most important players in this process. Our data clearly indicate that the CsLPCATs present in developing seeds have the potential to transfer almost all polyunsaturated fatty acids synthesised on phosphatidylcholine to the acyl-CoA pool. CsLPCAT activity is the highest at 30°C, and the enzymes operate well at a pH of 7.0–11.0, with the best activity at a pH of 9.0. The activity of CsLPCATs was inhibited by calcium and magnesium ions at a concentration of 0.05–2 mM. In the forward reaction, CsLPCATs preferentially utilise 18:2-CoA; however, other C18 unsaturated fatty acids are also well accepted. In the backward reactions, there is no clear discrimination between the C18 unsaturated fatty acids utilised by the enzymes for phosphatidylcholine remodelling. The activity of CsLPCATs does not differ much between the stages of seed development.
Main conclusion The transfer of polyunsaturated fatty acids from phosphatidylcholine to other lipids involves several enzymes. In Camelina sativa seeds, acyl-CoA:lysophosphatidylcholine acyltransferases could be one of the most important players in this process. The transfer of polyunsaturated fatty acids from the location of their synthesis (phosphatidylcholine) to other lipids, e.g., triacylglycerol, remains insufficiently understood. Several enzymes could be involved in this process. One of these enzymes is acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs). In Camelina sativa seeds, LPCATs could be one of the most important players in this process. Our data clearly indicate that the Cs LPCATs present in developing seeds have the potential to transfer almost all polyunsaturated fatty acids synthesised on phosphatidylcholine to the acyl-CoA pool. Cs LPCAT activity is the highest at 30 °C, and the enzymes operate well at a pH of 7.0–11.0, with the best activity at a pH of 9.0. The activity of Cs LPCATs was inhibited by calcium and magnesium ions at a concentration of 0.05–2 mM. In the forward reaction, Cs LPCATs preferentially utilise 18:2-CoA; however, other C18 unsaturated fatty acids are also well accepted. In the backward reactions, there is no clear discrimination between the C18 unsaturated fatty acids utilised by the enzymes for phosphatidylcholine remodelling. The activity of Cs LPCATs does not differ much between the stages of seed development.
Author Klińska, Sylwia
Jasieniecka-Gazarkiewicz, Katarzyna
Banaś, Antoni
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Cites_doi 10.1194/jlr.R800035-JLR200
10.1186/s13068-016-0555-5
10.1199/tab.0161
10.1042/bj1320697
10.1016/j.phytochem.2011.11.022
10.1016/S0005-2736(00)00135-8
10.4141/P04-081
10.1371/journal.pone.0144653
10.1016/j.pbi.2009.04.003
10.1016/j.indcrop.2013.07.042
10.1152/physiol.00019.2008
10.1104/pp.16.01865
10.1104/pp.118.1.183
10.1016/j.febslet.2007.12.020
10.1006/abbi.1996.0282
10.1016/j.pbi.2009.04.013
10.1073/pnas.120067297
10.1007/s11745-015-4102-0
10.1007/s11745-003-1110-0
10.1074/jbc.M115.654798
10.1016/S0926-6690(96)00203-8
10.1139/y59-099
10.1007/BF00203655
10.1104/pp.91.4.1288
10.1007/BF02534953
10.1111/j.1467-7652.2009.00427.x
10.1042/bst0280703
10.1074/jbc.M600225200
10.1073/pnas.0709737104
10.1146/annurev.pp.42.060191.002343
10.1042/bst0280715
10.1111/pbi.12679
10.1016/0003-9861(86)90726-5
10.1074/jbc.M113.521815
10.1104/pp.112.204438
10.1016/0005-2760(83)90076-0
10.1042/bj2230305
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Keywords False flax
TAG biosynthesis
Phosphatidylcholine remodelling
Triacylglycerol
Seed lipids
Acyl-CoA:lysophosphatidylcholine acyltransferases
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References Shindou, Hishikawa, Harayama, Yuki, Shimizu (CR30) 2009; 50
Kennedy (CR17) 1961; 20
Zhang, Jasieniecka-Gazarkiewicz, Wan, Luo, Zhang, Banaś, Jiang, Gong (CR38) 2015; 10
Jasieniecka-Gazarkiewicz, Demski, Lager, Stymne, Banaś (CR15) 2016; 51
Sánchez, David, David (CR29) 1973; 132
Zubr (CR40) 1997; 6
Lager, Yilmaz, Zhou, Jasieniecka, Kazachkov, Wang, Zou, Weselake, Smith, Bayon (CR18) 2013; 288
Pan, Chen, Kazachkov, Greer, Caldo, Zou, Weselake (CR25) 2015; 290
Gugel, Falk (CR13) 2006; 86
Engeseth, Pacovskya, Newman, Ohlrogge (CR10) 1996; 331
Rodriguez-Rodriguez, Sanchez-Garcia, Salas, Garces, Martínez-Force (CR27) 2013; 50
Stymne, Glad (CR34) 1981; 16
Putnam, Budin, Field, Breene, Janick, Simon (CR26) 1993
Browse, Somerville (CR7) 1991; 42
Bao, Pollard, Ohlrogge (CR3) 1998; 118
Furukawa-Stoffer, Boyl, Thomson, Sarna, Weselake (CR12) 2003; 38
Ruiz-Lopez, Usher, Salas, Haslam, Napier, Beaudoin (CR28) 2016; 15
Karley, White (CR16) 2009; 12
Constantinides, Steim (CR8) 1986; 250
Stymne, Stobart (CR35) 1984; 223
Ichihara, Mae, Sano, Tanaka (CR14) 1995; 196
Oo, Huang (CR24) 1989; 91
Slack, Campbell, Browse, Roughan (CR31) 1983; 754
Tumaney, Rajasekharan (CR36) 1999; 1439
Zheng, Li, Kazachkov, Liu, Zou (CR39) 2012; 75
Moomaw, Maguire (CR22) 2008; 23
Nakanishi, Shindou, Hishikawa, Harayama, Ogasawara, Suwabe, Taguchi, Shimizu (CR23) 2006; 281
Soupene, Fyrst, Kuypers (CR32) 2008; 105
Ståhl, Stålberg, Stymne, Ronne (CR33) 2008; 582
Maathuis (CR20) 2009; 12
Marmon, Sturtevant, Herrfurth, Chapman, Stymne, Feussner (CR21) 2017; 173
Li-Beisson, Shorrosh, Beisson, Andersson, Arondel, Bates, Baud, Debono, Durrett (CR19) 2013; 11
Bligh, Dyer (CR5) 1959; 37
Yurchenko, Nykiforuk, Moloney, Ståhl, Banaś, Stymne, Weselake (CR37) 2009; 7
Blumwald, Aharon, Apse (CR6) 2000; 1465
Dahlqvist, Ståhl, Lenman, Banaś, Lee, Sandager, Ronne, Stymne (CR9) 2000; 97
Abdullah, Akbari, Paulose, Schnell, Qi, Park, Pareek, Dhankher (CR1) 2016; 9
Banaś, Dahlqvist, Ståhl, Lenman, Stymne (CR2) 2000; 28
Bates, Fatihi, Snapp, Carlsson, Browse, Lu (CR4) 2012; 160
Fraser, Stobart (CR11) 2000; 28
S Stymne (3248_CR34) 1981; 16
A Banaś (3248_CR2) 2000; 28
KC Oo (3248_CR24) 1989; 91
FJM Maathuis (3248_CR20) 2009; 12
AS Moomaw (3248_CR22) 2008; 23
E Blumwald (3248_CR6) 2000; 1465
T Fraser (3248_CR11) 2000; 28
AW Tumaney (3248_CR36) 1999; 1439
HM Abdullah (3248_CR1) 2016; 9
NJ Engeseth (3248_CR10) 1996; 331
EP Kennedy (3248_CR17) 1961; 20
D Zhang (3248_CR38) 2015; 10
EG Bligh (3248_CR5) 1959; 37
DH Putnam (3248_CR26) 1993
CR Slack (3248_CR31) 1983; 754
Y Li-Beisson (3248_CR19) 2013; 11
M Sánchez (3248_CR29) 1973; 132
U Ståhl (3248_CR33) 2008; 582
Q Zheng (3248_CR39) 2012; 75
X Pan (3248_CR25) 2015; 290
PP Constantinides (3248_CR8) 1986; 250
PD Bates (3248_CR4) 2012; 160
I Lager (3248_CR18) 2013; 288
S Marmon (3248_CR21) 2017; 173
RK Gugel (3248_CR13) 2006; 86
K Jasieniecka-Gazarkiewicz (3248_CR15) 2016; 51
Broughton R Ruiz-Lopez (3248_CR28) 2016; 15
H Nakanishi (3248_CR23) 2006; 281
MF Rodriguez-Rodriguez (3248_CR27) 2013; 50
OP Yurchenko (3248_CR37) 2009; 7
X Bao (3248_CR3) 1998; 118
A Dahlqvist (3248_CR9) 2000; 97
H Shindou (3248_CR30) 2009; 50
E Soupene (3248_CR32) 2008; 105
J Browse (3248_CR7) 1991; 42
J Zubr (3248_CR40) 1997; 6
K Ichihara (3248_CR14) 1995; 196
AJ Karley (3248_CR16) 2009; 12
TL Furukawa-Stoffer (3248_CR12) 2003; 38
S Stymne (3248_CR35) 1984; 223
References_xml – volume: 50
  start-page: 46
  year: 2009
  end-page: 51
  ident: CR30
  article-title: Recent progress on acyl CoA:lysophospholipid acyltransferase research
  publication-title: J Lipid Res
  doi: 10.1194/jlr.R800035-JLR200
  contributor:
    fullname: Shimizu
– volume: 9
  start-page: 136
  year: 2016
  ident: CR1
  article-title: Transcriptome profiling of to identify genes involved in triacylglycerol biosynthesis and accumulation in the developing seeds
  publication-title: Biotechnol Biofuels
  doi: 10.1186/s13068-016-0555-5
  contributor:
    fullname: Dhankher
– volume: 11
  start-page: e0161
  year: 2013
  ident: CR19
  article-title: Acyl-lipid metabolism
  publication-title: Arabidopsis Book
  doi: 10.1199/tab.0161
  contributor:
    fullname: Durrett
– volume: 132
  start-page: 697
  year: 1973
  end-page: 706
  ident: CR29
  article-title: The relationship between palmitoyl-coenzyme A synthetase activity and esterification of sn-glycerol 3-phosphate in rat liver mitochondria
  publication-title: Biochem J
  doi: 10.1042/bj1320697
  contributor:
    fullname: David
– volume: 75
  start-page: 21
  year: 2012
  end-page: 31
  ident: CR39
  article-title: Identification of   lysophosphatidylcholine acyltransferase genes through yeast functional screening
  publication-title: Phytochemistry
  doi: 10.1016/j.phytochem.2011.11.022
  contributor:
    fullname: Zou
– volume: 1465
  start-page: 140
  issue: 1–2
  year: 2000
  end-page: 151
  ident: CR6
  article-title: Sodium transport in plant cells
  publication-title: Biochem Biophys Acta
  doi: 10.1016/S0005-2736(00)00135-8
  contributor:
    fullname: Apse
– volume: 86
  start-page: 1047
  year: 2006
  end-page: 1058
  ident: CR13
  article-title: Agronomic and seed quality evaluation of in western Canada
  publication-title: Can J Plant Sci
  doi: 10.4141/P04-081
  contributor:
    fullname: Falk
– volume: 10
  start-page: e0144653
  issue: 12
  year: 2015
  ident: CR38
  article-title: Molecular characterization of two lysophospholipid:acyl-CoA acyltransferases belonging to the MBOAT family in
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0144653
  contributor:
    fullname: Gong
– volume: 12
  start-page: 250
  year: 2009
  end-page: 258
  ident: CR20
  article-title: Physiological functions of mineral macronutrients
  publication-title: Curr Opin Plant Biol
  doi: 10.1016/j.pbi.2009.04.003
  contributor:
    fullname: Maathuis
– volume: 50
  start-page: 673
  year: 2013
  end-page: 679
  ident: CR27
  article-title: Characterization of the morphological changes and fatty acid profile of developing seeds
  publication-title: Ind Crops Prod
  doi: 10.1016/j.indcrop.2013.07.042
  contributor:
    fullname: Martínez-Force
– volume: 23
  start-page: 275
  year: 2008
  end-page: 285
  ident: CR22
  article-title: The unique nature of Mg channels
  publication-title: Physiology
  doi: 10.1152/physiol.00019.2008
  contributor:
    fullname: Maguire
– volume: 173
  start-page: 2081
  year: 2017
  end-page: 2095
  ident: CR21
  article-title: Two acyltransferases contribute differently to linolenic acid levels in seed oil
  publication-title: Plant Physiol
  doi: 10.1104/pp.16.01865
  contributor:
    fullname: Feussner
– volume: 118
  start-page: 183
  issue: 1
  year: 1998
  end-page: 190
  ident: CR3
  article-title: The biosynthesis of erucic acid in developing embryos of
  publication-title: Plant Physiol
  doi: 10.1104/pp.118.1.183
  contributor:
    fullname: Ohlrogge
– volume: 582
  start-page: 305
  year: 2008
  end-page: 309
  ident: CR33
  article-title: A family of eukaryotic lysophospholipid acyltransferases with broad specificity
  publication-title: FEBS Lett
  doi: 10.1016/j.febslet.2007.12.020
  contributor:
    fullname: Ronne
– volume: 331
  start-page: 55
  issue: 1
  year: 1996
  end-page: 62
  ident: CR10
  article-title: Characterization of an acyl-CoA-binding protein from
  publication-title: Arch Biochem Biophys
  doi: 10.1006/abbi.1996.0282
  contributor:
    fullname: Ohlrogge
– volume: 12
  start-page: 291
  year: 2009
  end-page: 298
  ident: CR16
  article-title: Moving cationic minerals to edible tissues: potassium, magnesium, calcium
  publication-title: Curr Opin Plant Biol
  doi: 10.1016/j.pbi.2009.04.013
  contributor:
    fullname: White
– volume: 97
  start-page: 6487
  year: 2000
  end-page: 6492
  ident: CR9
  article-title: Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants
  publication-title: Proc Natl Acad Sci USA
  doi: 10.1073/pnas.120067297
  contributor:
    fullname: Stymne
– volume: 51
  start-page: 15
  year: 2016
  end-page: 23
  ident: CR15
  article-title: Possible role of different yeast and plant lysophospholipid:acyl-CoA acyltransferases (LPLATs) in acyl remodelling of phospholipids
  publication-title: Lipids
  doi: 10.1007/s11745-015-4102-0
  contributor:
    fullname: Banaś
– volume: 38
  start-page: 651
  year: 2003
  end-page: 656
  ident: CR12
  article-title: Properties of lysophosphatidylcholine acyltransferase from cultures
  publication-title: Lipids
  doi: 10.1007/s11745-003-1110-0
  contributor:
    fullname: Weselake
– volume: 290
  start-page: 18068
  year: 2015
  end-page: 18078
  ident: CR25
  article-title: In vivo and in vitro evidence for biochemical coupling of reactions catalyzed by lysophosphatidylcholine acyltransferase and diacylglycerol acyltransferase
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M115.654798
  contributor:
    fullname: Weselake
– volume: 1439
  start-page: 47
  year: 1999
  end-page: 56
  ident: CR36
  article-title: Synthesis of azidophospholipids and labeling of lysophosphatidylcholine acyltransferase from developing soybean cotyledons
  publication-title: Biochem Biophys Acta
  contributor:
    fullname: Rajasekharan
– volume: 6
  start-page: 113
  year: 1997
  end-page: 119
  ident: CR40
  article-title: Oil-seed crop:
  publication-title: Ind Crops Prod
  doi: 10.1016/S0926-6690(96)00203-8
  contributor:
    fullname: Zubr
– volume: 37
  start-page: 911
  year: 1959
  end-page: 917
  ident: CR5
  article-title: A rapid method of total lipid extraction and purification
  publication-title: Can J Biochem Physiol
  doi: 10.1139/y59-099
  contributor:
    fullname: Dyer
– volume: 196
  start-page: 551
  year: 1995
  end-page: 557
  ident: CR14
  article-title: 1-Acyl-glycerophosphocholine -acyltransferase in maturing safflower seeds
  publication-title: Planta
  doi: 10.1007/BF00203655
  contributor:
    fullname: Tanaka
– volume: 91
  start-page: 1288
  year: 1989
  end-page: 1295
  ident: CR24
  article-title: Lysophosphatidate acyltransferase activities in the microsomes from palm endosperm, maize scutellum, and rapeseed cotyledon of maturing seeds
  publication-title: Plant Physiol
  doi: 10.1104/pp.91.4.1288
  contributor:
    fullname: Huang
– volume: 16
  start-page: 298
  year: 1981
  end-page: 305
  ident: CR34
  article-title: Acyl exchange between oleoyl-CoA and phosphatidylcholine in microsomes of developing soya bean cotyledons and its role in fatty acid desaturation
  publication-title: Lipids
  doi: 10.1007/BF02534953
  contributor:
    fullname: Glad
– volume: 7
  start-page: 602
  year: 2009
  end-page: 610
  ident: CR37
  article-title: A 10-kDa acyl-CoA-binding protein (ACBP) from Brassica napus enhances acyl exchange between acyl-CoA and phosphatidylcholine
  publication-title: Plant Biotechnol J
  doi: 10.1111/j.1467-7652.2009.00427.x
  contributor:
    fullname: Weselake
– volume: 28
  start-page: 703
  year: 2000
  end-page: 705
  ident: CR2
  article-title: The involvement of phospholipid:diacylglycerol acyltransferases in triacylglycerol production
  publication-title: Biochem Soc Trans
  doi: 10.1042/bst0280703
  contributor:
    fullname: Stymne
– volume: 281
  start-page: 20140
  year: 2006
  end-page: 20147
  ident: CR23
  article-title: Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1) expression in alveolar type ii cells and possible involvement in surfactant production
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M600225200
  contributor:
    fullname: Shimizu
– volume: 105
  start-page: 88
  issue: 1
  year: 2008
  end-page: 93
  ident: CR32
  article-title: Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes
  publication-title: Proc Natl Acad Sci USA
  doi: 10.1073/pnas.0709737104
  contributor:
    fullname: Kuypers
– volume: 42
  start-page: 467
  year: 1991
  end-page: 506
  ident: CR7
  article-title: Glycerolipid synthesis: biochemistry and regulation
  publication-title: Annu Rev Plant Physiol Plant Mol Biol
  doi: 10.1146/annurev.pp.42.060191.002343
  contributor:
    fullname: Somerville
– volume: 28
  start-page: 715
  issue: 6
  year: 2000
  end-page: 718
  ident: CR11
  article-title: Partial purification and photoaffinity labelling of sunflower acyl-CoA:lysophosphatidylcholine acyltransferase
  publication-title: Biochem Soc Trans
  doi: 10.1042/bst0280715
  contributor:
    fullname: Stobart
– volume: 20
  start-page: 934
  year: 1961
  end-page: 940
  ident: CR17
  article-title: Biosynthesis of complex lipids
  publication-title: Fed Proc
  contributor:
    fullname: Kennedy
– volume: 15
  start-page: 837
  year: 2016
  end-page: 849
  ident: CR28
  article-title: Tailoring the composition of novel wax esters in the seeds of transgenic through systematic metabolic engineering
  publication-title: Plant Biotechnol J
  doi: 10.1111/pbi.12679
  contributor:
    fullname: Beaudoin
– start-page: 314
  year: 1993
  end-page: 322
  ident: CR26
  article-title: : a promising low-input oilseed
  publication-title: New crops
  contributor:
    fullname: Simon
– volume: 250
  start-page: 267
  year: 1986
  end-page: 270
  ident: CR8
  article-title: Solubility of palmitoyl-coenzyme A in acyltransferase assay buffers containing magnesium ions
  publication-title: Arch Biochem Biophys
  doi: 10.1016/0003-9861(86)90726-5
  contributor:
    fullname: Steim
– volume: 288
  start-page: 36902
  issue: 52
  year: 2013
  end-page: 36914
  ident: CR18
  article-title: Plant acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have different specificities in their forward and reverse reactions
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M113.521815
  contributor:
    fullname: Bayon
– volume: 160
  start-page: 1530
  year: 2012
  end-page: 1539
  ident: CR4
  article-title: Acyl editing and headgroup exchange are the major mechanisms that direct polyunsaturated fatty acid flux into triacylglycerols
  publication-title: Plant Physiol
  doi: 10.1104/pp.112.204438
  contributor:
    fullname: Lu
– volume: 754
  start-page: 10
  year: 1983
  end-page: 20
  ident: CR31
  article-title: Some evidence for the reversibility of the cholinephosphotransferase-catalysed reaction in developing linseed cotyledons in vivo
  publication-title: Biochem Biophys Acta
  doi: 10.1016/0005-2760(83)90076-0
  contributor:
    fullname: Roughan
– volume: 223
  start-page: 305
  year: 1984
  end-page: 314
  ident: CR35
  article-title: Evidence for the reversibility of the acyl-CoA:lysophosphatidylcholine acyltransferase in microsomal preparations from developing safflower ( L.) cotyledons and rat liver
  publication-title: Biochem J
  doi: 10.1042/bj2230305
  contributor:
    fullname: Stobart
– volume: 28
  start-page: 703
  year: 2000
  ident: 3248_CR2
  publication-title: Biochem Soc Trans
  doi: 10.1042/bst0280703
  contributor:
    fullname: A Banaś
– volume: 97
  start-page: 6487
  year: 2000
  ident: 3248_CR9
  publication-title: Proc Natl Acad Sci USA
  doi: 10.1073/pnas.120067297
  contributor:
    fullname: A Dahlqvist
– volume: 75
  start-page: 21
  year: 2012
  ident: 3248_CR39
  publication-title: Phytochemistry
  doi: 10.1016/j.phytochem.2011.11.022
  contributor:
    fullname: Q Zheng
– volume: 1439
  start-page: 47
  year: 1999
  ident: 3248_CR36
  publication-title: Biochem Biophys Acta
  contributor:
    fullname: AW Tumaney
– volume: 331
  start-page: 55
  issue: 1
  year: 1996
  ident: 3248_CR10
  publication-title: Arch Biochem Biophys
  doi: 10.1006/abbi.1996.0282
  contributor:
    fullname: NJ Engeseth
– volume: 15
  start-page: 837
  year: 2016
  ident: 3248_CR28
  publication-title: Plant Biotechnol J
  doi: 10.1111/pbi.12679
  contributor:
    fullname: Broughton R Ruiz-Lopez
– volume: 582
  start-page: 305
  year: 2008
  ident: 3248_CR33
  publication-title: FEBS Lett
  doi: 10.1016/j.febslet.2007.12.020
  contributor:
    fullname: U Ståhl
– volume: 38
  start-page: 651
  year: 2003
  ident: 3248_CR12
  publication-title: Lipids
  doi: 10.1007/s11745-003-1110-0
  contributor:
    fullname: TL Furukawa-Stoffer
– volume: 250
  start-page: 267
  year: 1986
  ident: 3248_CR8
  publication-title: Arch Biochem Biophys
  doi: 10.1016/0003-9861(86)90726-5
  contributor:
    fullname: PP Constantinides
– volume: 6
  start-page: 113
  year: 1997
  ident: 3248_CR40
  publication-title: Ind Crops Prod
  doi: 10.1016/S0926-6690(96)00203-8
  contributor:
    fullname: J Zubr
– volume: 132
  start-page: 697
  year: 1973
  ident: 3248_CR29
  publication-title: Biochem J
  doi: 10.1042/bj1320697
  contributor:
    fullname: M Sánchez
– volume: 7
  start-page: 602
  year: 2009
  ident: 3248_CR37
  publication-title: Plant Biotechnol J
  doi: 10.1111/j.1467-7652.2009.00427.x
  contributor:
    fullname: OP Yurchenko
– volume: 196
  start-page: 551
  year: 1995
  ident: 3248_CR14
  publication-title: Planta
  doi: 10.1007/BF00203655
  contributor:
    fullname: K Ichihara
– volume: 20
  start-page: 934
  year: 1961
  ident: 3248_CR17
  publication-title: Fed Proc
  contributor:
    fullname: EP Kennedy
– volume: 23
  start-page: 275
  year: 2008
  ident: 3248_CR22
  publication-title: Physiology
  doi: 10.1152/physiol.00019.2008
  contributor:
    fullname: AS Moomaw
– volume: 42
  start-page: 467
  year: 1991
  ident: 3248_CR7
  publication-title: Annu Rev Plant Physiol Plant Mol Biol
  doi: 10.1146/annurev.pp.42.060191.002343
  contributor:
    fullname: J Browse
– volume: 12
  start-page: 250
  year: 2009
  ident: 3248_CR20
  publication-title: Curr Opin Plant Biol
  doi: 10.1016/j.pbi.2009.04.003
  contributor:
    fullname: FJM Maathuis
– volume: 86
  start-page: 1047
  year: 2006
  ident: 3248_CR13
  publication-title: Can J Plant Sci
  doi: 10.4141/P04-081
  contributor:
    fullname: RK Gugel
– volume: 50
  start-page: 673
  year: 2013
  ident: 3248_CR27
  publication-title: Ind Crops Prod
  doi: 10.1016/j.indcrop.2013.07.042
  contributor:
    fullname: MF Rodriguez-Rodriguez
– volume: 754
  start-page: 10
  year: 1983
  ident: 3248_CR31
  publication-title: Biochem Biophys Acta
  doi: 10.1016/0005-2760(83)90076-0
  contributor:
    fullname: CR Slack
– volume: 16
  start-page: 298
  year: 1981
  ident: 3248_CR34
  publication-title: Lipids
  doi: 10.1007/BF02534953
  contributor:
    fullname: S Stymne
– volume: 160
  start-page: 1530
  year: 2012
  ident: 3248_CR4
  publication-title: Plant Physiol
  doi: 10.1104/pp.112.204438
  contributor:
    fullname: PD Bates
– volume: 10
  start-page: e0144653
  issue: 12
  year: 2015
  ident: 3248_CR38
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0144653
  contributor:
    fullname: D Zhang
– volume: 11
  start-page: e0161
  year: 2013
  ident: 3248_CR19
  publication-title: Arabidopsis Book
  doi: 10.1199/tab.0161
  contributor:
    fullname: Y Li-Beisson
– volume: 51
  start-page: 15
  year: 2016
  ident: 3248_CR15
  publication-title: Lipids
  doi: 10.1007/s11745-015-4102-0
  contributor:
    fullname: K Jasieniecka-Gazarkiewicz
– volume: 1465
  start-page: 140
  issue: 1–2
  year: 2000
  ident: 3248_CR6
  publication-title: Biochem Biophys Acta
  doi: 10.1016/S0005-2736(00)00135-8
  contributor:
    fullname: E Blumwald
– volume: 12
  start-page: 291
  year: 2009
  ident: 3248_CR16
  publication-title: Curr Opin Plant Biol
  doi: 10.1016/j.pbi.2009.04.013
  contributor:
    fullname: AJ Karley
– volume: 91
  start-page: 1288
  year: 1989
  ident: 3248_CR24
  publication-title: Plant Physiol
  doi: 10.1104/pp.91.4.1288
  contributor:
    fullname: KC Oo
– volume: 50
  start-page: 46
  year: 2009
  ident: 3248_CR30
  publication-title: J Lipid Res
  doi: 10.1194/jlr.R800035-JLR200
  contributor:
    fullname: H Shindou
– volume: 9
  start-page: 136
  year: 2016
  ident: 3248_CR1
  publication-title: Biotechnol Biofuels
  doi: 10.1186/s13068-016-0555-5
  contributor:
    fullname: HM Abdullah
– volume: 173
  start-page: 2081
  year: 2017
  ident: 3248_CR21
  publication-title: Plant Physiol
  doi: 10.1104/pp.16.01865
  contributor:
    fullname: S Marmon
– volume: 290
  start-page: 18068
  year: 2015
  ident: 3248_CR25
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M115.654798
  contributor:
    fullname: X Pan
– volume: 223
  start-page: 305
  year: 1984
  ident: 3248_CR35
  publication-title: Biochem J
  doi: 10.1042/bj2230305
  contributor:
    fullname: S Stymne
– volume: 288
  start-page: 36902
  issue: 52
  year: 2013
  ident: 3248_CR18
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M113.521815
  contributor:
    fullname: I Lager
– volume: 105
  start-page: 88
  issue: 1
  year: 2008
  ident: 3248_CR32
  publication-title: Proc Natl Acad Sci USA
  doi: 10.1073/pnas.0709737104
  contributor:
    fullname: E Soupene
– volume: 37
  start-page: 911
  year: 1959
  ident: 3248_CR5
  publication-title: Can J Biochem Physiol
  doi: 10.1139/y59-099
  contributor:
    fullname: EG Bligh
– volume: 118
  start-page: 183
  issue: 1
  year: 1998
  ident: 3248_CR3
  publication-title: Plant Physiol
  doi: 10.1104/pp.118.1.183
  contributor:
    fullname: X Bao
– start-page: 314
  volume-title: New crops
  year: 1993
  ident: 3248_CR26
  contributor:
    fullname: DH Putnam
– volume: 28
  start-page: 715
  issue: 6
  year: 2000
  ident: 3248_CR11
  publication-title: Biochem Soc Trans
  doi: 10.1042/bst0280715
  contributor:
    fullname: T Fraser
– volume: 281
  start-page: 20140
  year: 2006
  ident: 3248_CR23
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M600225200
  contributor:
    fullname: H Nakanishi
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Snippet The transfer of polyunsaturated fatty acids from the location of their synthesis (phosphatidylcholine) to other lipids, e.g., triacylglycerol, remains...
Main conclusion The transfer of polyunsaturated fatty acids from phosphatidylcholine to other lipids involves several enzymes. In Camelina sativa seeds,...
The transfer of polyunsaturated fatty acids from phosphatidylcholine to other lipids involves several enzymes. In Camelina sativa seeds,...
Main conclusionThe transfer of polyunsaturated fatty acids from phosphatidylcholine to other lipids involves several enzymes. In Camelina sativa seeds,...
MAIN CONCLUSIONThe transfer of polyunsaturated fatty acids from phosphatidylcholine to other lipids involves several enzymes. In Camelina sativa seeds,...
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SubjectTerms 1-Acylglycerophosphocholine O-Acyltransferase - genetics
1-Acylglycerophosphocholine O-Acyltransferase - metabolism
Agriculture
Biomedical and Life Sciences
Brassicaceae - enzymology
Brassicaceae - genetics
Brassicaceae - growth & development
Calcium
Camelina sativa
Developmental stages
Ecology
Enzymes
Fatty acids
Forestry
Lecithin
Life Sciences
Lipids
Lysophosphatidylcholine
Magnesium
ORIGINAL ARTICLE
pH effects
Phosphatidylcholine
Plant Proteins - genetics
Plant Proteins - metabolism
Plant Sciences
Polyunsaturated fatty acids
Seeds
Seeds - enzymology
Seeds - genetics
Seeds - growth & development
Triglycerides
Subtitle lysophosphatidylcholine acyltransferases (LPCATs) of Camelina sativa seeds: biochemical properties and function
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Title Acyl-CoA
URI https://www.jstor.org/stable/48702380
https://link.springer.com/article/10.1007/s00425-019-03248-6
https://www.ncbi.nlm.nih.gov/pubmed/31407031
https://www.proquest.com/docview/2272048328/abstract/
https://search.proquest.com/docview/2272736452
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