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Information on EC 2.3.1.B36 - glycerophosphocholine O-acyltransferase
for references in articles please use BRENDA:EC2.3.1.B36preliminary BRENDA-supplied EC number
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EC Tree
2.3.1.B36 glycerophosphocholine O-acyltransferaseSpecify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
glycerophosphocholine acyltransferase, gpc1p, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl-CoA:glycerophosphocholine acyltransferase
glycerophosphocholine acyltransferase
glycerophosphocholine acyltransferase 1
GPC1
Gpc1p
GPCAT
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:glycerophosphocholine O-acyltransferase
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-oleoyl-sn-glycero-3-phosphatidic acid + glycerophosphocholine
glycero-3-phosphatidic acid + 1-oleoyl-sn-glycero-3-phosphocholine
very low activity compared to lysphosphatidylcholine
-
-
?
1-oleoyl-sn-glycero-3-phosphocholine + glycerophosphocholine
glycero-3-phosphocholine + 1-oleoyl-sn-glycero-3-phosphocholine
best lysolipid substrate
-
-
?
1-oleoyl-sn-glycero-3-phosphoethanolamine + glycerophosphocholine
glycero-3-phosphoethanolamine + 1-oleoyl-sn-glycero-3-phosphocholine
moderate activity compared to lysphosphatidylcholine
-
-
?
1-oleoyl-sn-glycero-3-phosphoserine + glycerophosphocholine
glycero-3-phosphoserine + 1-oleoyl-sn-glycero-3-phosphocholine
low activity compared to lysphosphatidylcholine
-
-
?
oleoyl-CoA + glycerophosphoethanolamine
CoA + 1-oleoyl-sn-glycero-3-phosphoethanolamine
enzyme Gpc1p also catalyzes the acylation of GPE with acyl-CoA, with about one third of activity compared to glycerophosphocholine
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
linolenoyl-CoA + glycerophosphocholine
CoA + 1-linolenoyl-sn-glycero-3-phosphocholine
-
best substrate
-
-
?
linolenoyl-CoA + glycerophosphocholine
CoA + 1-linolenoyl-sn-glycero-3-phosphocholine
-
best substrate
-
-
?
linolenoyl-CoA + glycerophosphocholine
CoA + 1-linolenoyl-sn-glycero-3-phosphocholine
-
best substrate
-
-
?
linolenoyl-CoA + glycerophosphocholine
CoA + 1-linolenoyl-sn-glycero-3-phosphocholine
-
best substrate
-
-
?
linolenoyl-CoA + glycerophosphocholine
CoA + 1-linolenoyl-sn-glycero-3-phosphocholine
-
best substrate
-
-
?
linolenoyl-CoA + glycerophosphocholine
CoA + 1-linolenoyl-sn-glycero-3-phosphocholine
high activity
-
-
?
linolenoyl-CoA + glycerophosphocholine
CoA + 1-linolenoyl-sn-glycero-3-phosphocholine
high activity
-
-
?
linolenoyl-CoA + glycerophosphocholine
CoA + 1-linolenoyl-sn-glycero-3-phosphocholine
high activity
-
-
?
linolenoyl-CoA + glycerophosphocholine
CoA + 1-linolenoyl-sn-glycero-3-phosphocholine
-
best substrate
-
-
?
linoleoyl-CoA + glycerophosphocholine
CoA + 1-linoleoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
linoleoyl-CoA + glycerophosphocholine
CoA + 1-linoleoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
linoleoyl-CoA + glycerophosphocholine
CoA + 1-linoleoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
linoleoyl-CoA + glycerophosphocholine
CoA + 1-linoleoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
linoleoyl-CoA + glycerophosphocholine
CoA + 1-linoleoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
linoleoyl-CoA + glycerophosphocholine
CoA + 1-linoleoyl-sn-glycero-3-phosphocholine
high activity
-
-
?
linoleoyl-CoA + glycerophosphocholine
CoA + 1-linoleoyl-sn-glycero-3-phosphocholine
high activity
-
-
?
linoleoyl-CoA + glycerophosphocholine
CoA + 1-linoleoyl-sn-glycero-3-phosphocholine
high activity
-
-
?
linoleoyl-CoA + glycerophosphocholine
CoA + 1-linoleoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
oleoyl-CoA + glycerophosphocholine
CoA + 1-oleoyl-sn-glycero-3-phosphocholine
high activity
-
-
?
oleoyl-CoA + glycerophosphocholine
CoA + 1-oleoyl-sn-glycero-3-phosphocholine
moderate activity
-
-
?
palmitoleoyl-CoA + glycerophosphocholine
CoA + 1-palmitoleoyl-sn-glycero-3-phosphocholine
moderate activity
-
-
?
palmitoleoyl-CoA + glycerophosphocholine
CoA + 1-palmitoleoyl-sn-glycero-3-phosphocholine
moderate activity
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
radioactive assay with [14C]16:0-CoA
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
radioactive assay with [14C]16:0-CoA
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
radioactive assay with [14C]16:0-CoA
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
radioactive assay with [14C]16:0-CoA
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
high activity, best substrate
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
radioactive assay with [14C]16:0-CoA
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
high activity, best substrate
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
high activity, best substrate
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
radioactive assay with [14C]16:0-CoA
-
-
?
ricinoleoyl-CoA + glycerophosphocholine
CoA + 1-ricinoleoyl-sn-glycero-3-phosphocholine
moderate activity
-
-
?
ricinoleoyl-CoA + glycerophosphocholine
CoA + 1-ricinoleoyl-sn-glycero-3-phosphocholine
high activity
-
-
?
stearoyl-CoA + glycerophosphocholine
CoA + 1-stearoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
stearoyl-CoA + glycerophosphocholine
CoA + 1-stearoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
stearoyl-CoA + glycerophosphocholine
CoA + 1-stearoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
stearoyl-CoA + glycerophosphocholine
CoA + 1-stearoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
stearoyl-CoA + glycerophosphocholine
CoA + 1-stearoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
stearoyl-CoA + glycerophosphocholine
CoA + 1-stearoyl-sn-glycero-3-phosphocholine
moderate activity
-
-
?
stearoyl-CoA + glycerophosphocholine
CoA + 1-stearoyl-sn-glycero-3-phosphocholine
moderate activity
-
-
?
stearoyl-CoA + glycerophosphocholine
CoA + 1-stearoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
additional information
?
-
acyl-CoA substrate specificty of GCP1p with glycerophosphocholine, overview
-
-
-
additional information
?
-
lysolipids can also serve as acyl donor substrates for ScGPCAT (Gpc1p) activity. ScGPCAT acyl-CoA substrate specificity and transacylation activity of GPCAT, overview
-
-
-
additional information
?
-
-
lysolipids can also serve as acyl donor substrates for ScGPCAT (Gpc1p) activity. ScGPCAT acyl-CoA substrate specificity and transacylation activity of GPCAT, overview
-
-
-
additional information
?
-
lysolipids can also serve as acyl donor substrates for ScGPCAT (Gpc1p) activity. ScGPCAT acyl-CoA substrate specificity and transacylation activity of GPCAT, overview
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + glycerophosphocholine
CoA + 1-acyl-sn-glycero-3-phosphocholine
-
-
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
-
-
?
palmitoyl-CoA + glycerophosphocholine
CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
-
-
-
?
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.032
pH 7.2, 30°C, with substrates palmitoyl-CoA and glycerophosphocholine
0.038
about, pH 7.2, 30°C, with substrates palmitoyl-CoA and glycerophosphocholine
0.052
pH 7.2, 30°C, with substrates palmitoyl-CoA and glycerophosphocholine
0.086
pH 7.2, 30°C, with substrates palmitoyl-CoA and glycerophosphocholine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Gpc1p is an intergral membrane protein with eight transmembrane helices
brenda
-
Gpc1p is an intergral membrane protein with eight transmembrane helices
-
brenda
microsomal preparations from castor bean seeds have high GPCAT activity
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
evolution of the GPCAT family in eukaryotes, phylogenetic tree, evolutionary analysis, overview. GPCAT does not show any significant homology to other known acyl transferases and constitutes an enzyme family on its own with homologues represented in major eukaryotic organism groups but absent in prokaryotes
evolution
evolution of the GPCAT family in eukaryotes, phylogenetic tree, evolutionary analysis, overview. GPCAT does not show any significant homology to other known acyl transferases and constitutes an enzyme family on its own with homologues represented in major eukaryotic organism groups but absent in prokaryotes
evolution
evolution of the GPCAT family in eukaryotes, phylogenetic tree, evolutionary analysis, overview. GPCAT does not show any significant homology to other known acyl transferases and constitutes an enzyme family on its own with homologues represented in major eukaryotic organism groups but absent in prokaryotes
evolution
evolution of the GPCAT family in eukaryotes, phylogenetic tree, evolutionary analysis, overview. GPCAT does not show any significant homology to other known acyl transferases and constitutes an enzyme family on its own with homologues represented in major eukaryotic organism groups but absent in prokaryotes
evolution
-
evolution of the GPCAT family in eukaryotes, phylogenetic tree, evolutionary analysis, overview. GPCAT does not show any significant homology to other known acyl transferases and constitutes an enzyme family on its own with homologues represented in major eukaryotic organism groups but absent in prokaryotes
-
metabolism
-
the enzyme provides a distinct route of resynthesising phosphatidylcholine via lysophosphatidylcholine after its deacylation. This route does not require the degradation of the glycerophosphocholine into free choline, the activation of choline to CDP-choline, nor the utilization of CDP-choline by the CDP-choline:diacylglycerol cholinephosphotransferase. GPCAT activity plays a ubiquitous role inplant lipid metabolism
metabolism
-
the enzyme provides a novel route of resynthesising phosphatidylcholine via lysophosphatidylcholine after its deacylation. This route does not require the degradation of the glycerophosphocholine into free choline, the activation of choline to CDP-choline, nor the utilization of CDP-choline by the CDP-choline:diacylglycerol cholinephosphotransferase. GPCAT activity plays a ubiquitous role inplant lipid metabolism
metabolism
-
the enzyme provides a novel route of resynthesising phosphatidylcholine via lysophosphatidylcholine after its deacylation. This route does not require the degradation of the glycerophosphocholine into free choline, the activation of choline to CDP-choline, nor the utilization of CDP-choline by the CDP-choline:diacylglycerol cholinephosphotransferase. GPCAT activity plays a ubiquitous role inplant lipid metabolism
metabolism
-
the enzyme provides a novel route of resynthesising phosphatidylcholine via lysophosphatidylcholine after its deacylation. This route does not require the degradation of the glycerophosphocholine into free choline, the activation of choline to CDP-choline, nor the utilization of CDP-choline by the CDP-choline:diacylglycerol cholinephosphotransferase. GPCAT activity plays a ubiquitous role inplant lipid metabolism
metabolism
-
the enzyme provides a novel route of resynthesising phosphatidylcholine via lysophosphatidylcholine after its deacylation. This route does not require the degradation of the glycerophosphocholine into free choline, the activation of choline to CDP-choline, nor the utilization of CDP-choline by the CDP-choline:diacylglycerol cholinephosphotransferase. GPCAT activity plays a ubiquitous role inplant lipid metabolism
metabolism
-
the enzyme provides a novel route of resynthesising phosphatidylcholine via lysophosphatidylcholine after its deacylation. This route does not require the degradation of the glycerophosphocholine into free choline, the activation of choline to CDP-choline, nor the utilization of CDP-choline by the CDP-choline:diacylglycerol cholinephosphotransferase. GPCAT activity plays a ubiquitous role inplant lipid metabolism
physiological function
-
glycerophosphocholine:acyl-CoA acyltransferase (GPCAT) activity provides a distinct direct route of phosphatidylcholine resynthesis via lysophosphatidylcholine following its deacylation. GPCAT and not acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) is the limiting step in the formation of phosphatidylcholine
physiological function
-
glycerophosphocholine:acyl-CoA acyltransferase (GPCAT) activity provides a distinct direct route of phosphatidylcholine resynthesis via lysophosphatidylcholine following its deacylation. GPCAT and not acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT), which is catalyzing the next step in the pathway, is the limiting step in the formation of phosphatidylcholine
physiological function
-
glycerophosphocholine:acyl-CoA acyltransferase (GPCAT) activity provides a distinct direct route of phosphatidylcholine resynthesis via lysophosphatidylcholine following its deacylation. GPCAT and not acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT), which is catalyzing the next step in the pathway, is the limiting step in the formation of phosphatidylcholine
physiological function
-
glycerophosphocholine:acyl-CoA acyltransferase (GPCAT) activity provides a distinct direct route of phosphatidylcholine resynthesis via lysophosphatidylcholine following its deacylation. GPCAT and not acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT), which is catalyzing the next step in the pathway, is the limiting step in the formation of phosphatidylcholine
physiological function
-
glycerophosphocholine:acyl-CoA acyltransferase (GPCAT) activity provides a distinct direct route of phosphatidylcholine resynthesis via lysophosphatidylcholine following its deacylation. GPCAT and not acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT), which is catalyzing the next step in the pathway, is the limiting step in the formation of phosphatidylcholine
physiological function
-
glycerophosphocholine:acyl-CoA acyltransferase (GPCAT) activity provides a distinct direct route of phosphatidylcholine resynthesis via lysophosphatidylcholine following its deacylation. GPCAT and not acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT), which is catalyzing the next step in the pathway, is the limiting step in the formation of phosphatidylcholine
physiological function
cellular role for Gpc1p in the synthesis of phosphocholine via acylation of GPC. GPCAT is also unique in that it has, in addition to acyl-CoA acyltransferase activity, LPC:GPC transacylase activity
physiological function
cellular role for Gpc1p in the synthesis of phosphocholine via acylation of GPC. GPCAT is also unique in that it has, in addition to acyl-CoA acyltransferase activity, LPC:GPC transacylase activity
physiological function
cellular role for Gpc1p in the synthesis of phosphocholine via acylation of GPC. GPCAT is also unique in that it has, in addition to acyl-CoA acyltransferase activity, LPC:GPC transacylase activity
physiological function
cellular role for Gpc1p in the synthesis of phosphocholine via acylation of GPC. GPCAT is also unique in that it has, in addition to acyl-CoA acyltransferase activity, LPC:GPC transacylase activity
physiological function
-
cellular role for Gpc1p in the synthesis of phosphocholine via acylation of GPC. GPCAT is also unique in that it has, in addition to acyl-CoA acyltransferase activity, LPC:GPC transacylase activity
-
additional information
-
GPCAT enzyme activity in microsomal membrane preparations from Arabidopsis thaliana roots and leaves occurs at much lower activity level compared to oil seed membranes, e.g. from safflower (Carthamus tinctorius), castor bean (Ricinus communis), elm (Ulmus glabra), and rape seed (Brassica napus)
additional information
-
GPCAT enzyme activity in microsomal membrane preparations from Brassica napus oil seeds occurs at about 50% lower activity level compared to oil seed membranes from safflower (Carthamus tinctorius), castor bean (Ricinus communis), and elm (Ulmus glabra)
additional information
-
GPCAT enzyme activity in microsomal membrane preparations from Crambe abyssinica oil seeds occurs at much lower activity level compared to oil seed membranes from safflower (Carthamus tinctorius), castor bean (Ricinus communis), and elm (Ulmus glabra)
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GPC1_RICCO
391
0
45744
Swiss-Prot
Secretory Pathway (Reliability: 2)
GPC1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
432
0
51647
Swiss-Prot
other Location (Reliability: 1)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
plant homologues of GPC1 catalyze acyl-CoA-dependent acylation of GPC when expressed in yeast. Identification of a deletion strain lacking GPCAT activity, but exhibiting glycerol 3-phosphate (G3P) acylation. The identified strain bears a deletion in ORF YGR149W encoding GPC1. Wild-type GPC1 complements the deletion strain
additional information
-
plant homologues of GPC1 catalyze acyl-CoA-dependent acylation of GPC when expressed in yeast. Identification of a deletion strain lacking GPCAT activity, but exhibiting glycerol 3-phosphate (G3P) acylation. The identified strain bears a deletion in ORF YGR149W encoding GPC1. Wild-type GPC1 complements the deletion strain
additional information
-
plant homologues of GPC1 catalyze acyl-CoA-dependent acylation of GPC when expressed in yeast. Identification of a deletion strain lacking GPCAT activity, but exhibiting glycerol 3-phosphate (G3P) acylation. The identified strain bears a deletion in ORF YGR149W encoding GPC1. Wild-type GPC1 complements the deletion strain
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GPC1 or At5g35460, sequence comparisons, functional recombinant expression in Saccharoymces cerevisiae
gene GPC1 or BnaA04g07370D, sequence comparisons, functional recombinant expression in Saccharoymces cerevisiae
gene GPC1 or XM_002514040, sequence comparisons, functional recombinant expression in Saccharoymces cerevisiae
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lager, I.; Glab, B.; Eriksson, L.; Chen, G.; Banas, A.; Stymne, S.
Novel reactions in acyl editing of phosphatidylcholine by lysophosphatidylcholine transacylase (LPCT) and acyl-CoA:glycerophosphocholine acyltransferase (GPCAT) activities in microsomal preparations of plant tissues
Planta
241
347-358
2015
Arabidopsis thaliana, Brassica napus, Carthamus tinctorius, Ricinus communis, Crambe hispanica subsp. abyssinica, Ulmus glabra
brenda
Glab, B.; Beganovic, M.; Anaokar, S.; Hao, M.S.; Rasmusson, A.G.; Patton-Vogt, J.; Banas, A.; Stymne, S.; Lager, I.
Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and plants a novel enzyme phosphatidylcholine synthesis
J. Biol. Chem.
291
25066-25076
2016
Brassica napus (A0A078H868), Ricinus communis (B9RK42), Saccharomyces cerevisiae (P48236), Saccharomyces cerevisiae, Arabidopsis thaliana (Q9FJB4), Saccharomyces cerevisiae ATCC 204508 (P48236)
brenda
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Release 2023.1 (January 2023)
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