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Information on EC 2.7.8.2 - diacylglycerol cholinephosphotransferase
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EC Tree
2.7.8.2 diacylglycerol cholinephosphotransferaseIUBMB Comments
1-Alkyl-2-acylglycerol can act as acceptor; this activity was previously listed separately.
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Word Map
- 2.7.8.2
- diacylglycerols
- acyltransferase
- phosphatidylethanolamine
- cytidylyltransferase
- phospholipase
- phosphatidate
- cdpcholine
-
platelet-activating
-
ctp:phosphocholine
- 1,2-diacylglycerols
-
cholinephosphate
- cmp
- cdp-ethanolamine
- lysophosphatidylcholine
- glycerolipids
- glycerophospholipids
-
14ccholine
- 1,2-diacyl-sn-glycerols
-
ptdcho
-
acetylhydrolase
-
disaturated
- lysolecithin
-
lyso-paf
-
kennedy
- paf-ah
-
phosphotransferases
-
2.7.7.15
-
3hcholine
-
cdp-alcohol
-
methyl-3hcholine
-
alkylacylglycerols
- glycerolphosphate
-
methyl-14ccholine
- 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine
-
phosphatidyltransferase
- paf-acetylhydrolase
- phosphoglycerides
- synthesis
- analysis
- biotechnology
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cholinephosphotransferase, choline phosphotransferase, cept1, paf-cpt, dtt-insensitive cholinephosphotransferase, diacylglycerol cholinephosphotransferase, phosphorylcholine glyceride transferase, 1,2-diacylglycerol cholinephosphotransferase, aapt1, phosphatidylcholine:diacylglycerol cholinephosphotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-alkyl-2-acetyl-m-glycerol:CDP-choline choline phosphotransferase
-
-
-
-
1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase
-
-
-
-
1-alkyl-2-acetylglycerol cholinephosphotransferase
-
-
-
-
AAPT
-
-
-
-
alkylacylglycerol choline phosphotransferase
-
-
-
-
alkylacylglycerol cholinephosphotransferase
-
-
-
-
aminoalcoholphosphotransferase
CDP-choline diglyceride phosphotransferase
-
-
-
-
CEPT
CEPT1
choline phosphotransferase
cholinephosphotransferase
cholinephosphotransferase, 1-alkyl-2-acetylglycerol
-
-
-
-
cholinephosphotransferase, diacylglycerol
-
-
-
-
CPT
CPT1
cytidine diphosphocholine glyceride transferase
-
-
-
-
cytidine diphosphorylcholine diglyceride transferase
-
-
-
-
diacylglycerol choline phosphotransferase
-
-
-
-
DTT-insensitive CDP-choline: 1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase
-
-
EC 2.7.8.16
-
-
formerly
-
PAF-CPT
-
PAF: platelet activating factor, to be distinguished from PC-CPT, PC: phosphatidylcholine
PDCT
PDCT1
PDCT2
phosphatidylcholine diacylglycerol cholinephosphotransferase
phosphatidylcholine:diacylglycerol cholinephosphotransferase
-
-
phosphocholine diacylglyceroltransferase
-
-
-
-
phospholipid:diacylglycerol choline phosphotransferase
-
phosphorylcholine-glyceride transferase
-
-
-
-
sn-1,2-diacylglycerol cholinephosphotransferase
-
-
-
-
TDE0021
aminoalcoholphosphotransferase
-
-
-
-
CEPT
-
-
-
-
cholinephosphotransferase
-
-
-
-
CPT
-
-
-
-
phosphatidylcholine diacylglycerol cholinephosphotransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine
sequential kinetic mechanism
-
CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine
chimeric constructs of cholinephosphotransferase and choline/ethanolaminephosphotransferase, study on mechanism of cation activation
-
CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine
1-alkyl-2-acylglycerol can act as acceptor, this activity was previously listed as EC 2.7.8.16, 1-alkyl-2-acylglycerol choline phosphotransferase
-
-
-
CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine
mechanism of regulation by thyroid hormone T3
-
CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine
bi-bi sequential mechanism involving a direct nucleophilic attack of diacylglycerol on CDP-choline during the reaction
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
substituted phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
CDP-choline:1,2-diacyl-sn-glycerol cholinephosphotransferase
1-Alkyl-2-acylglycerol can act as acceptor; this activity was previously listed separately.
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CAS REGISTRY NUMBER
COMMENTARY
77237-98-0
formerly, EC 2.7.8.16
9026-13-5
-
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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
3-alpha-D-glucopyranosyl-1,2-di-palmitoylglycerol + CDP-choline
CMP + 3-(6-O-cholinephosphoryl-alpha-D-glucopyranosyl)-1,2-dipalmitoylglycerol
CDP-choline + 1,2-dilinolenoyl-sn-glycerol
CMP + 1,2-dilinolenoylphosphatidylcholine
-
-
-
-
?
CDP-choline + 1,2-dioleoyl-sn-glycerol
?
-
the most preferred diacylglycerol substrate is 18:0/20:4 diacylglycerol, followed by 18:0/22:6 diacylglycerol. The specific activities for 18:0/20:4 diacylglycerol and 18:0/22:6 diacylglycerol are 26 and 14fold higher than those of other diacylglycerol species
-
-
?
CDP-choline + 1,2-dioleoyl-sn-glycerol
CMP + 1,2-dioleoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
CDP-choline + 1,2-dipalmitoyl-sn-glycerol
CMP + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
CDP-choline + 1-arachidoyl-2-oleoyl-sn-glycerol
CMP + 1-arachidoyl-2-oleoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + 1-batyl-2-acetyl-sn-glycerol
CMP + 1-batyl-2-acetyl-sn-glycero-3-phosphocholine
-
-
-
-
?
CDP-choline + 1-chimyl-2-acetyl-sn-glycerol
CMP + 1-chimyl-2-acetyl-sn-glycero-3-phosphocholine
-
-
-
-
?
CDP-choline + 1-heptadecanoyl-2-oleoyl-sn-glycerol
CMP + 1-heptadecanoyl-2-oleoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + 1-hexadecanoyl-2-octadecanoyl-sn-glycerol
CMP + 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
CDP-choline + 1-hexadecyl-2-acetyl-sn-glycerol
CMP + 1-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine
-
-
-
-
?
CDP-choline + 1-hexadecyl-2-octadecanoyl-sn-glycerol
CMP + 1-hexadecyl-2-octadecanoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
CDP-choline + 1-hexadecyl-2-octadecenoyl-sn-glycerol
CMP + 1-hexadecyl-2-octadecenoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
CDP-choline + 1-lauroyl-2-oleoyl-sn-glycerol
CMP + 1-lauroyl-2-oleoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + 1-myristoyl-2-oleoyl-sn-glycerol
CMP + 1-myristoyl-2-oleoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + 1-nonadecanoyl-2-oleoyl-sn-glycerol
CMP + 1-nonadecanoyl-2-oleoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + 1-O-alkyl-2-acetyl-sn-glycerol
CMP + 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine
CDP-choline + 1-O-hexadecyl-2-acetyl-sn-glycerol
CMP + 1-O-hexadecyl-2-acetyl-sn-glycero-phosphocholine
-
-
-
-
?
CDP-choline + 1-palmitoyl-2-linoleoylglycerol
CMP + 1-palmitoyl-2-linoleoylglycero-3-phosphocholine
CDP-choline + 1-palmitoyl-2-oleoyl-sn-glycerol
CMP + 1-palmitoyl-2-oleoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + 1-pentadecanoyl-2-oleoyl-sn-glycerol
CMP + 1-pentadecanoyl-2-oleoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + 1-selachyl-2-acetyl-sn-glycerol
CMP + 1-selachyl-2-acetyl-sn-glycero-3-phosphocholine
-
-
-
-
?
CDP-choline + 1-stearoyl-2-oleoyl-sn-glycerol
CMP + 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
CDP-choline + 1-stearoyl-2-oleoyl-sn-glycerol
CMP + 1-stearoyl-2-oleoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + 1-tridecanoyl-2-oleoyl-sn-glycerol
CMP + 1-tridecanoyl-2-oleoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + bacterial 1,2-diacyl-sn-glycerol
CMP + phosphatidylethanolamine
-
-
-
-
?
CDP-choline + didodecanoylglycerol
CMP + didodecanoylglycerophosphocholine
-
-
-
-
?
CDP-choline + dimyristoyl-sn-glycerol
CMP + dimyristoyl-sn-glycerophosphocholine
-
-
-
-
?
CDP-choline + dioctanoylglycerol
CMP + dioctanoylglycerophosphocholine
-
at 5-10% of the activity with dioleoylglycerol or egg diglycerides
-
-
?
CMP + a phosphatidylcholine
CDP-choline + 1,2-diacylglycerol
-
-
-
r
dCDP-choline + 1,2-diacylglycerol
CMP + 1,2-diacylglycero-3-phosphocholine
-
-
-
-
?
3-alpha-D-glucopyranosyl-1,2-di-palmitoylglycerol + CDP-choline
CMP + 3-(6-O-cholinephosphoryl-alpha-D-glucopyranosyl)-1,2-dipalmitoylglycerol
-
-
-
?
3-alpha-D-glucopyranosyl-1,2-di-palmitoylglycerol + CDP-choline
CMP + 3-(6-O-cholinephosphoryl-alpha-D-glucopyranosyl)-1,2-dipalmitoylglycerol
-
-
-
?
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
enzyme phosphatidylcholine diacylglycerol cholinephosphotransferase catalyzes the interconversion between phosphatidylcholine and diacylglycerol
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
r
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
preferred substrates in decreasing order: di-10:0 diacylglycerol, di-16:1 diacylglycerol, di-8:0 diacylglycerol, di-18:1 diacylglycerol, 16:0/22:6 diacylglycerol
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
preferred substrates in decreasing order, activation by Mg2+: di18:1-diacylglycerol, 16:0/22:6-diacylglycerol, 16:0/18:1-diacylglycerol, 18:0/20:4-diacylglycerol, di16:0-diacylglycerol, preferred substrates in decreasing order, activation by Mn2+: di10:0-diacylglycerol, 18:1/2:0-diacylglycerol, 16:0/22:6-diacylglycerol, di18:1-diacylglycerol, di16:0-diacylglycerol, di14:1-diacylglycerol, di16:1-diacylglycerol
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
preferred substrates: di-18:1-diacylglycerol, di-16:1-diacylglycerol, 16:0/18:1-diacylglycerol, 16:0/22:6-diacylglycerol
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
-
-
?
CDP-choline + 1,2-dipalmitoyl-sn-glycerol
CMP + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
-
preferred substrate over other disaturated species
-
-
?
CDP-choline + 1,2-dipalmitoyl-sn-glycerol
CMP + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
-
poor substrate
-
-
?
CDP-choline + 1-O-alkyl-2-acetyl-sn-glycerol
CMP + 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine
-
platelet activating factor (PAF) de novo biosynthesis
-
-
?
CDP-choline + 1-O-alkyl-2-acetyl-sn-glycerol
CMP + 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine
-
37°C, 20 min, pH 8, in presence of 15 mM dithiothreitol, 5 mM EDTA, 20 mM MgCl2, 1 mg/ml bovine serum albumin
analysis by thin-layer chromatography
-
?
CDP-choline + 1-palmitoyl-2-linoleoylglycerol
CMP + 1-palmitoyl-2-linoleoylglycero-3-phosphocholine
-
preferred substrate
-
-
?
CDP-choline + 1-palmitoyl-2-linoleoylglycerol
CMP + 1-palmitoyl-2-linoleoylglycero-3-phosphocholine
-
preferred substrate
-
-
?
CDP-choline + didecanoylglycerol
CMP + didecanoylglycerophosphocholine
-
-
-
-
?
CDP-choline + didecanoylglycerol
CMP + didecanoylglycerophosphocholine
-
at 5-10% of the activity with dioleoylglycerol or egg diglycerides
-
-
?
CDP-choline + dihexanoylglycerol
CMP + dihexanoylglycerophosphocholine
-
-
-
-
?
CDP-choline + dihexanoylglycerol
CMP + dihexanoylglycerophosphocholine
-
at 5-10% of the activity with dioleoylglycerol or egg diglycerides
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
dithiothreitol-sensitive activity
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
dithiothreitol-sensitive activity
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
dithiothreitol-sensitive activity
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
r
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylethanolamine
-
-
-
r
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylethanolamine
-
-
-
r
CDP-ethanolamine + 1,2-diacylglycerol
CMP + phosphatidylethanolamine
-
-
-
r
CDP-ethanolamine + 1,2-diacylglycerol
CMP + phosphatidylethanolamine
-
preferred substrates in decreasing order: di-18:1 diacylglycerol, di-16:1 diacylglycerol, 16:0/18:1 diacylglycerol, 16:0/22:6 diacylglycerol
-
-
?
CDP-ethanolamine + 1,2-diacylglycerol
CMP + phosphatidylethanolamine
-
preferred substrates: 16:0/18:1 diacylglycerol, di-18:1 diacylglycerol, di-18:1 diacylglycerol
-
-
?
CMP + phosphatidylcholine
?
-
principal pathway for degradation of phosphatidylcholine, particularly during brain ischemia, followed by hydrolysis of diacylglycerols by the lipase
-
-
?
CMP + phosphatidylcholine
CDP-choline + 1,2-diacylglycerol
-
-
-
-
r
CMP + phosphatidylcholine
CDP-choline + 1,2-diacylglycerol
-
-
-
-
r
additional information
?
-
-
little or no specificity across a range of different diacylglycerol substrates
-
-
?
additional information
?
-
-
PDCT accepts substrates with different desaturation levels. PDCT is unable to use diacylglycerols with ricineoleyl groups, and the presence of this substrate also inhibits PDCT from using other diacylglycerol moieties
-
-
-
additional information
?
-
-
little or no specificity across a range of different diacylglycerol substrates
-
-
?
additional information
?
-
-
significant preference for unsaturated diacylglycerols over saturated sialylglycerols
-
-
?
additional information
?
-
-
little or no specificity across a range of different diacylglycerol substrates
-
-
?
additional information
?
-
the enzyme has dual specificity for both CDP-choline and CDP-ethanolamine, EC 2.7.8.1
-
-
?
additional information
?
-
-
lacks specificity for the type of diglyceride
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
the enzyme is specific for CDP-choline, no activity with CDP-ethanolamine. The reaction occurs at the hydrophobic-hydrophilic interface of membranes which impacts kinetic behavior
-
-
?
additional information
?
-
no substrates: 16:0(O)/2:0-diacylglycerol, 16:0(O)/20:4-diacylglycerol
-
-
?
additional information
?
-
-
no substrates: 16:0(O)/2:0-diacylglycerol, 16:0(O)/20:4-diacylglycerol
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
increase in cholinephosphotransferase gene expression with cadmium in all cell lines, significant increase in 11-9-1-4 cells and MCF-12F cells. Cell lines MCF-12F, MCF-7, BT-549 and 11-9-1-4 show mutations in their nucleotide sequence as the result of cadmium treatment. The effect of cadmium is highest in MCF-12F cell line that shows a total of six mutations
-
-
?
additional information
?
-
the enzyme has dual specificity for both CDP-choline and CDP-ethanolamine, EC 2.7.8.1
-
-
?
additional information
?
-
the enzyme has dual specificity for both CDP-choline and CDP-ethanolamine, EC 2.7.8.1
-
-
?
additional information
?
-
the enzyme is specific for CDP-choline, no activity with CDP-ethanolamine. The reaction occurs at the hydrophobic-hydrophilic interface of membranes which impacts kinetic behavior
-
-
?
additional information
?
-
the enzyme is specific for CDP-choline, no activity with CDP-ethanolamine. The reaction occurs at the hydrophobic-hydrophilic interface of membranes which impacts kinetic behavior
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
renal mRNA expression of cholinephosphotransferase 1 may be involved in the development and/or progression of diabetic nephropathy
-
-
?
additional information
?
-
-
role of enzyme in de novo and remodeling pathways
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
higher activity with 16:0 and 18:1 substrates than with 18:0 substrates
-
-
?
additional information
?
-
-
influence of saturated fatty acids on the enzyme activities depends on their location at the C-1 or C-2 position of glycerol
-
-
?
additional information
?
-
-
no substrate: 1,3-diC18:1-glycerol ether
-
-
?
additional information
?
-
-
no substrate: 1,2-diC18:1-glycerol ether
-
-
?
additional information
?
-
-
1-acyl-2-oleoylglycerols, ranging from 1-lauroyl to 1-heptadecanoyl species are equally well utilized, fully saturated diacylglycerols like dipalmitoylglycerol are poorly utilized, several 1-oleoyl-2-saturated types of diacylglycerol are effectively used
-
-
?
additional information
?
-
-
dithiothreitol-insensitive enzyme prefers a lipid substrate with 16:0 or 18:1 sn-1-alkyl chains
-
-
?
additional information
?
-
-
short chain esters at the sn-2 position (acetate or propionate) are utilized
-
-
?
additional information
?
-
-
a marked preference of the enzyme for the 1-palmitoyl over the 1-stearoyl homologue is observed with all 4 unsaturation classes of diacylglycerols
-
-
?
additional information
?
-
-
substrates are 1,2-diacylglycerols containing fatty acids 6, 12 and 14 carbons in length
-
-
?
additional information
?
-
-
no substrate: analogs with acetamide or methoxy substituents at the sn-2-position
-
-
?
additional information
?
-
-
the reversibility of phosphoethanolamine transferase and phosphocholine transferase permits the interconversion of diacylglycerol moieties of choline and ethanolamine glycerophospholipids
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
renal dithiothreitol-insensitive enzyme could be a potentially important enzyme in the regulation of systemic blood pressure
-
-
?
additional information
?
-
-
last step in de novo synthesis of diacylglycerophosphocholine
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
significant selectivity which may be of considerable importance in maintaining the characteristic composition of fatty acyl chains in membrane phospholipids
-
-
?
additional information
?
-
-
little or no specificity across a range of different diacylglycerol substrates
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
the enzyme is specific for CDP-choline, no activity with CDP-ethanolamine. The reaction occurs at the hydrophobic-hydrophilic interface of membranes which impacts kinetic behavior
-
-
?
additional information
?
-
-
the enzyme is specific for CDP-choline, no activity with CDP-ethanolamine. The reaction occurs at the hydrophobic-hydrophilic interface of membranes which impacts kinetic behavior
-
-
?
additional information
?
-
-
lipogenic enzyme is involved in biosynthesis of triacylglycerol. The low dietary n-3/n-6 polyunsaturated fatty acid ratio presented in the vegetable oil diet does not sifnificantly affect enzyme activity
-
-
?
additional information
?
-
-
no selectivity towards the molecular species of the endogenous pool of diacylglycerols
-
-
?
additional information
?
-
-
utilizes 1-myristyl phosphatidylcholine most rapidly and, in decreasing order the 1-palmitoyl and 1-stearyl species
-
-
?
additional information
?
-
-
utilizes without marked selectivity the endogenous 1,2-diacylglycerol species differing in the degree of unsaturation
-
-
?
additional information
?
-
-
dithiothreitol-insensitive activity
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
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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
3-alpha-D-glucopyranosyl-1,2-di-palmitoylglycerol + CDP-choline
CMP + 3-(6-O-cholinephosphoryl-alpha-D-glucopyranosyl)-1,2-dipalmitoylglycerol
CDP-choline + 1-O-alkyl-2-acetyl-sn-glycerol
CMP + 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine
-
platelet activating factor (PAF) de novo biosynthesis
-
-
?
3-alpha-D-glucopyranosyl-1,2-di-palmitoylglycerol + CDP-choline
CMP + 3-(6-O-cholinephosphoryl-alpha-D-glucopyranosyl)-1,2-dipalmitoylglycerol
-
-
-
?
3-alpha-D-glucopyranosyl-1,2-di-palmitoylglycerol + CDP-choline
CMP + 3-(6-O-cholinephosphoryl-alpha-D-glucopyranosyl)-1,2-dipalmitoylglycerol
-
-
-
?
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
enzyme phosphatidylcholine diacylglycerol cholinephosphotransferase catalyzes the interconversion between phosphatidylcholine and diacylglycerol
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + sn-1,2-diacylglycerol
?
-
dithiothreitol-sensitive activity
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
dithiothreitol-sensitive activity
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
dithiothreitol-sensitive activity
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
r
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylethanolamine
-
-
-
r
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylethanolamine
-
-
-
r
CMP + phosphatidylcholine
?
-
principal pathway for degradation of phosphatidylcholine, particularly during brain ischemia, followed by hydrolysis of diacylglycerols by the lipase
-
-
?
additional information
?
-
the enzyme has dual specificity for both CDP-choline and CDP-ethanolamine, EC 2.7.8.1
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
increase in cholinephosphotransferase gene expression with cadmium in all cell lines, significant increase in 11-9-1-4 cells and MCF-12F cells. Cell lines MCF-12F, MCF-7, BT-549 and 11-9-1-4 show mutations in their nucleotide sequence as the result of cadmium treatment. The effect of cadmium is highest in MCF-12F cell line that shows a total of six mutations
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
renal mRNA expression of cholinephosphotransferase 1 may be involved in the development and/or progression of diabetic nephropathy
-
-
?
additional information
?
-
-
role of enzyme in de novo and remodeling pathways
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
the reversibility of phosphoethanolamine transferase and phosphocholine transferase permits the interconversion of diacylglycerol moieties of choline and ethanolamine glycerophospholipids
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
renal dithiothreitol-insensitive enzyme could be a potentially important enzyme in the regulation of systemic blood pressure
-
-
?
additional information
?
-
-
last step in de novo synthesis of diacylglycerophosphocholine
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
significant selectivity which may be of considerable importance in maintaining the characteristic composition of fatty acyl chains in membrane phospholipids
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
lipogenic enzyme is involved in biosynthesis of triacylglycerol. The low dietary n-3/n-6 polyunsaturated fatty acid ratio presented in the vegetable oil diet does not sifnificantly affect enzyme activity
-
-
?
additional information
?
-
-
dithiothreitol-insensitive activity
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
additional information
Mg2+
activation, 10fold more than Mn2+, preferred substrates in decreasing order, activation by Mg2+: di18:1-diacylglycerol, 16:0/22:6-diacylglycerol, 16:0/18:1-diacylglycerol, 18:0/20:4-diacylglycerol, di16:0-diacylglycerol
Mg2+
-
requires Mg2+ rather than Mn2+, particularly at physiological concentrations less than 5 mM
Mg2+
-
Mg2+ is less effective than Mn2+ as cofactor in the reverse reaction
Mn2+
-
activates, acts mostly on ethanolaminephosphotransferase activity, inhibitory above 10 mM
Mn2+
activation, but much less than Mg2+, preferred substrates in decreasing order, activation by Mn2+: di10:0-diacylglycerol, 18:1/2:0-diacylglycerol, 16:0/22:6-diacylglycerol, di18:1-diacylglycerol, di16:0-diacylglycerol, di14:1-diacylglycerol, di16:1-diacylglycerol
Mn2+
-
Mg2+ is less effective than Mn2+ as cofactor in the reverse reaction
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cholate
-
inactivation at solubilization concentration, full recovery of activity after reconstituting the membrane by adding excess lipid and removing detergent by gel filtration, dialysis or absorption to Bio-Beads, if membrane is solubilized with octylglucoside or cholate at weight ratios of detergent:membrane protein of at least 10, the activity is irreversibly lost unless stabilizers are added with detergent, diacylglycerol and glycerol are effective stabilizers
INFalpha
-
250 inhibitory units/microl, 51% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
Phospholipids
-
phosphatidylcholine, phosphatidylethanolamine or lysophosphatidylethanolamine activates, lysophosphatidylcholine inhibits
polar lipids from olive oil
-
5.2 ng/microl, 33% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
polar lipids from olive pomace
-
1.8 ng/microl, 48% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
polar lipids from sea bass
-
59 ng/microl, 45% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
polar lipids from sea bream
-
123 ng/microl, 17% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
resveratrol
-
100 microM, 39% inhibition of enzyme activity in microsomal fraction of mesangial cells
rupatadine
-
20 ng/microl, 60% inhibition of enzyme activity in microsomal fraction of mesangial cells
salicylic acid
-
250 ng/microl, 38% inhibition of enzyme activity in microsomal fraction of mesangial cells
SDS
-
inactivation at solubilization concentration, full recovery of activity after reconstituting the membrane by adding excess lipid and removing detergent by gel filtration, dialysis or absorption to Bio-Beads
simvastatine
-
40 ng/microl, 92% inhibition of enzyme activity in microsomal fraction of mesangial cells
tinzaparin
-
0.25 inhibitory units/microl, 30% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
U-73122
-
phospholipase C inhibitor, inhibition reversed by prostaglandin D2
Ca2+
isoenzyme AAPT1, 30% inhibition at 0.1 mM, AAPT2, 18% inhibition at 0.1 mM
Ca2+
-
0.1 mM (14.1% activity left) or 1 mM (1.41% activity left), estimated in presence of 20 mM Mg2+, inhibition partially reduced in presence of 0.5 mM EDTA: 33.3% or 3.70% activity left for 0.1 mM or 1 mM Ca2+, respectively (100% activity: 20 mM Mg2+, 0.5 mM EDTA, no Ca2+)
Ca2+
-
half-maximal inhibition: 0.15 mM in presence of 5 mM Mg2+, half-maximal inhibition: 5 mM in presence of 5 mM Mn2+
CMP
isozyme AAPT1, 43% inhibition at 2 mM, AAPT2 14% inhibition at 2 mM
deoxycholate
-
stimulates at low subsolubilizing concentrations, membrane-solubilizing concentrations lead to nearly complete inactivation
dithiothreitol
-
slight enhancement of activity towards 1-alkyl-2-acetyl-sn-glycerol, inhibition of activity towards diacylglycerol
n-octylglucoside
-
inactivation at solubilization concentration, full recovery of activity after reconstituting the membrane by adding excess lipid and removing detergent by gel filtration, dialysis or absorption to Bio-Beads, if membrane is solubilized with octylglucoside or cholate at weight ratios of detergent:membrane protein of at least 10, the activity is irreversibly lost unless stabilizers are added with detergent, diacylglycerol and glycerol are effective stabilizers
Phospholipase A2
-
rapid inactivation, microsomal total phospholipids partially reactivate
-
Triton X-100
-
inactivation at solubilization concentration, full recovery of activity after reconstituting the membrane by adding excess lipid (soybean) and removing detergent by gel filtration, dialysis or absorption to Bio-Beads; X-100
Triton X-100
-
activity assayed with Mg2+ is more labile than that assayed with Mn2+; X-100
Tween-20
-
inactivation at solubilization concentration, full recovery of activity after reconstituting the membrane by adding excess lipid (soybean) and removing detergent by gel filtration, dialysis or absorption to Bio-Beads
Tween-20
-
stimulates at low subsolubilizing concentrations, membrane-solubilizing concentrations lead to nearly complete inactivation
additional information
-
inhibition of enzyme activity as a chronic effect of treatment with chloroethyl ethyl sulfide may be directly responsible for reduction in the lung surfactant production, resulting in subsequent development of acute respiratory distress syndrome and pulmonary fibrosis. Ceramide production induced by chloroethyl ethyl sulfide may play a direct role in the reduction of cholinephosphotransferase activity
-
additional information
detergent micelles that are used to deliver the DAG substrate for the assay can inhibit the reaction
-
additional information
detergent micelles that are used to deliver the DAG substrate for the assay can inhibit the reaction
-
additional information
detergent micelles that are used to deliver the DAG substrate for the assay can inhibit the reaction
-
additional information
-
heat-labile, nondialyzable endogenous inhibitor may act at the binding step of the enzyme to its lipid substrate
-
additional information
detergent micelles that are used to deliver the DAG substrate for the assay can inhibit the reaction
-
additional information
-
detergent micelles that are used to deliver the DAG substrate for the assay can inhibit the reaction
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
-
specific activity increases in presence of 0.5-2 mg/ml bovine serum albumin, microsomal fraction of human mesangial cells
-
ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid
-
stimulates
lysolecithin
-
stimulates at low subsolubilizing concentrations, membrane-solubilizing concentrations lead to nearly complete inactivation
Triton X-100
-
stimulates at low subsolubilizing concentrations, membrane-solubilizing concentrations lead to nearly complete inactivation
Tween-20
-
stimulates at low subsolubilizing concentrations, membrane-solubilizing concentrations lead to nearly complete inactivation
unsaturated fatty acids
-
a number of unsaturated fatty acids markedly stimulate, 0.8 mM oleate activates if a mixed diglyceride such as 1-palmitoyl-2-oleoyl-sn-glycerol is used as a substrate, dipalmitin or diolein incorporation into lecithin is not stimulated
-
additional information
-
cholinephosphotransferase requires a lipidic boundary for full activation, no activation by substrate
-
deoxycholate
-
stimulates at low subsolubilizing concentrations, membrane-solubilizing concentrations lead to nearly complete inactivation
dithiothreitol
-
specific activity slightly increases at dithiothreitol (DTT) concentrations above 1 mM, optimum stimulation at 15 mM DTT, microsomal fraction of human mesangial cells
dithiothreitol
-
slight enhancement of activity towards 1-alkyl-2-acetyl-sn-glycerol, inhibition of activity towards diacylglycerol
Phospholipids
-
phosphatidylcholine, phosphatidylethanolamine or lysophosphatidylethanolamine activates, lysophosphatidylcholine inhibits
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
Competitive inhibition of choline phosphotransferase by geranylgeraniol and farnesol inhibits phosphatidylcholine synthesis and induces apoptosis in human lung adenocarcinoma A549 cells.
Anemia, Hemolytic
A family with chronic haemolysis and selective accumulation of erythrocyte CDP-choline.
Anemia, Hemolytic
Red cell CDP (dCDP)-choline and P-choline in normal subjects and in certain hemolytic syndromes.
Brain Injuries
Effects of CDP-choline on phospholipase A2 and cholinephosphotransferase activities following a cryogenic brain injury in the rabbit.
Brain Ischemia
The reverse reaction of cholinephosphotransferase in rat brain microsomes. A new pathway for degradation of phosphatidylcholine.
Breast Neoplasms
Breast cancer is associated with an increase in the activity and expression of cholinephosphotransferase in rats.
Breast Neoplasms
Modulation of cholinephosphotransferase activity in breast cancer cell lines by Ro5-4864, a peripheral benzodiazepine receptor agonist.
Dengue
Rapid phospholipase A2 stimulation and diacylglycerol cholinephosphotransferase inhibition in baby hamster kidney cells during initiation of dengue virus infection.
diacylglycerol cholinephosphotransferase deficiency
Red cell CDP (dCDP)-choline and P-choline in normal subjects and in certain hemolytic syndromes.
Fatty Liver
Phosphatidylethanolamine-N-methyltransferase activity and dietary choline regulate liver-plasma lipid flux and essential fatty acid metabolism in mice.
Fatty Liver
Phospholipid transmethylation and choline phosphotransferase in microsomal fraction of human diseased liver.
Hepatitis
Phospholipid transmethylation and choline phosphotransferase in microsomal fraction of human diseased liver.
Hepatitis, Alcoholic
Phospholipid transmethylation and choline phosphotransferase in microsomal fraction of human diseased liver.
Hypercholesterolemia
Effect of hypercholesterolemia on cholinephosphotransferase activity in rabbit and rat vessel walls.
Hypertension, Renovascular
Role of platelet-activating factor in two-kidney, one-clip hypertension.
Hyperthyroidism
The effect of hyper and hypothyroidism, hypophysectomy and adrenalectomy on phosphatidylethanolamine methyltransferase, phosphatidyldimethyl-ethanolamine methyltransferase and choline phosphotransferase of rat liver microsomes.
Hypothyroidism
The effect of hyper and hypothyroidism, hypophysectomy and adrenalectomy on phosphatidylethanolamine methyltransferase, phosphatidyldimethyl-ethanolamine methyltransferase and choline phosphotransferase of rat liver microsomes.
Infections
Cholinephosphotransferase and ethanolaminephosphotransferase activities in Plasmodium knowlesi-infected erythrocytes. Their use as parasite-specific markers.
Infections
Increased production of the ether-lipid platelet-activating factor in intestinal epithelial cells infected by Salmonella enteritidis.
Infections
Influence of infection with an influenza A virus (fowl plague) on Ca++-uptake and lipid metabolism of chick embryo cells in culture.
Infections
Influence of the infection with lipid-containing viruses on the metabolism and pools of phospholipid precursors in animal cells.
Influenza in Birds
Influence of the infection with lipid-containing viruses on the metabolism and pools of phospholipid precursors in animal cells.
Insulin Resistance
Skeletal Muscle Phospholipid Metabolism Regulates Insulin Sensitivity and Contractile Function.
Leukemia
1-beta-D-arabinofuranosylcytosine-diphosphate-choline is formed by the reversal of cholinephosphotransferase and not via cytidylyltransferase.
Lung Injury
Inhibition of cholinephosphotransferase activity in lung injury induced by 2-chloroethyl ethyl sulfide, a mustard analog.
Neoplasms
Growth arrest and DNA damage-inducible 45? protects against nonalcoholic steatohepatitis induced by methionine- and choline-deficient diet.
Newcastle Disease
Influence of the infection with lipid-containing viruses on the metabolism and pools of phospholipid precursors in animal cells.
Obesity
Skeletal Muscle Phospholipid Metabolism Regulates Insulin Sensitivity and Contractile Function.
Peripheral Arterial Disease
CEPT1-Mediated Phospholipogenesis Regulates Endothelial Cell Function and Ischemia-Induced Angiogenesis Through PPAR?.
Respiratory Distress Syndrome
Familial respiratory distress syndrome in three consecutive full-term infants. Case reports and documentation of lung enzyme activities.
Seizures
Cerebellar metabolism of phosphatidylcholine and its hydrosoluble precursors during bicuculline-induced convulsive seizures.
Virus Diseases
Effect of Friend virus infection on the biosynthetic enzymes of phosphatidylcholine biosynthesis in spleen microsomes.
Virus Diseases
Rapid phospholipase A2 stimulation and diacylglycerol cholinephosphotransferase inhibition in baby hamster kidney cells during initiation of dengue virus infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0593
1-O-alkyl-2-acetyl-sn-glycerol
-
optimum reaction conditions, in presence of 100 microM CDP-choline
0.0166
CDP-choline
-
optimum reaction conditions, in presence of 100 microM 1-O-alkyl-2-acetyl-sn-glycerol
0.048
CDP-choline
-
cosubstrate 1-hexadecanoyl-2-octadecanoyl-sn-glycerol, pH 8.2, 30°C
0.053
CDP-choline
-
cosubstrate 1-hexadecyl-2-octadecenoyl-sn-glycerol, pH 8.2, 30°C
additional information
additional information
-
Km for CDP-choline, depends on diacylglycerol structure
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00036
-
microsomal fraction of human mesangial cells, maximum activity in presence of 1 mg/ml bovine serum albumin, 15 mM dithiothreitol, 20 mM Mg2+, 0.5 mM EDTA
additional information
additional information
-
linear relationship between initial velocity and protein concentration in microsomal fraction of human mesangial cells up to 0.1 mg/ml
additional information
-
Pefabloc has no affect on enzyme activity, microsomal fraction of human mesangial cells
additional information
-
0.8 nmol/mg protein, dimethylbenz(alpha)anthracene induced tumor
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
-
microsomal fraction of human mesangial cells (HMC), bell-shaped temperature activity profile
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and O82568, dual-specificity enzymes, activities of EC 2.7.8.1 and EC 2.7.8.2
SwissProt
brenda
dual-specificity enzyme, activitiy of EC 2.7.8.1 and EC 2.7.8.2
-
-
brenda
-
642888, 644322, 644323, 644324, 644327, 644328, 644329, 644330, 644331, 644334, 644338, 644339, 644343, 644345, 644349, 644355, 644356, 644357, 644358, 644360, 644362, 644363, 644365, 644372, 644374, 644375
-
-
brenda
dual-specificity enzyme, activitiy of EC 2.7.8.1 and EC 2.7.8.2
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
developing, the isozymes are both highly expressed during the mid to late stages, 8 to 16 days after anthesis, DAA, of embryo development, peaking at approximately 11 DAA with transcript levels decreasing dramatically after 16 DAA to nearly undetectable levels for the remainder of seed development
brenda
-
normal: MCF-12A and MCF-12F and cancerous: MCF-7, BT-549 and 11-9-1-4
brenda
-
HMC, immortilized by transfection with T-antigen of SV40 and Hras oncogene
brenda
additional information
CEPT1 is elevated in diseased lower extremity arterial intima of individuals with peripheral arterial disease and diabetes
brenda
CEPT1 is elevated in diseased lower extremity arterial intima of individuals with peripheral arterial disease and diabetes
brenda
CEPT1 is elevated in carotid plaque of patients with diabetes
brenda
CEPT1 is elevated in carotid plaque of patients with diabetes
brenda
CEPT1 is elevated in diseased lower extremity arterial intima of individuals with peripheral arterial disease and diabetes
brenda
CEPT1 is elevated in diseased lower extremity arterial intima of individuals with peripheral arterial disease and diabetes
brenda
-
activity levels of glomerular putative mCHPT1 in BALB/c mice tend to be slightly higher than those in type 2 diabetic KK/Ta mice
brenda
-
-
644322, 644323, 644324, 644327, 644334, 644339, 644343, 644356, 644357, 644358, 644362, 644363, 644365, 644375
brenda
additional information
-
seed oil composition of wild-type and enzyme-RNAi targeted mutant lines, overview
brenda
additional information
tissue-specific enzyme expression analysis by virtual expression analysis from RNASeq data
brenda
additional information
-
tissue-specific enzyme expression analysis by virtual expression analysis from RNASeq data
brenda
additional information
isozymes LuPDCT1 and LuPDCT2 exhibit similar spatiotemporal patterns of expression. Both LuPDCT1 and LuPDCT2 are expressed at very low levels in all vegetative and floral tissues tested, stem, leaves, shoot apex, root and flowers
brenda
additional information
isozymes LuPDCT1 and LuPDCT2 exhibit similar spatiotemporal patterns of expression. Both LuPDCT1 and LuPDCT2 are expressed at very low levels in all vegetative and floral tissues tested, stem, leaves, shoot apex, root and flowers
brenda
additional information
-
isozymes LuPDCT1 and LuPDCT2 exhibit similar spatiotemporal patterns of expression. Both LuPDCT1 and LuPDCT2 are expressed at very low levels in all vegetative and floral tissues tested, stem, leaves, shoot apex, root and flowers
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
-
644322, 644323, 644324, 644327, 644328, 644334, 644338, 644339, 644345, 644349, 644355, 644356, 644357, 644358, 644362, 644363, 644365
brenda
co-purifies with crude mitochondria during subcellular fractionation of organelles
-
brenda
co-purifies with crude mitochondria during subcellular fractionation of organelles
-
brenda
co-purifies with crude mitochondria during subcellular fractionation of organelles
-
brenda
additional information
-
no activity detectable in cytoplasmic fraction of mesangial cells
-
brenda
additional information
CPT/CEPT enzymes reside in multiple subcellular membranes that can move among organelles
-
brenda
additional information
CPT/CEPT enzymes reside in multiple subcellular membranes that can move among organelles
-
brenda
additional information
the enzyme localization is not altered upon treatment of cells with brefeldin A
-
brenda
additional information
the enzyme localization is not altered upon treatment of cells with brefeldin A
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
very low levels of hydroxy fatty acid are detected when FAH12 (fatty acid hydroxylase) is expressed in seeds of the Arabidopsis rod1 mutant, which contains a lesion in PDCT. A castor PDCT enzyme encoded by the RcROD1 gene increases hydroxy fatty acid levels when coexpressed with FAH12 (fatty acid hydroxylase)
malfunction
inhibition of the CPT activity reduces phospholipid synthesis and results in accumulation of CPT substrates. Reduction of phosphatidylcholine, e.g. by bacterial infection, results in apoptosis
malfunction
reduction of phosphatidylcholine, e.g. by bacterial infection, results in apoptosis
metabolism
CPT catalyzes the final step in the synthesis of phosphatidylcholine via the Kennedy pathway by the transfer of phosphocholine from CDP-choline to 1,2-diacyl-sn-glycerol. The CDP-choline and CDP-ethanolamine pathways are separate routes of phospholipid biosynthesis in mammalian cells, although the CEPT is probably a participant in both pathways
metabolism
CPT catalyzes the final step in the synthesis of phosphatidylcholine via the Kennedy pathway by the transfer of phosphocholine from CDP-choline to 1,2-diacyl-sn-glycerol. The CDP-choline and CDP-ethanolamine pathways are separate routes of phospholipid biosynthesis in mammalian cells, although the CEPT is probably a participant in both pathways
metabolism
CPT catalyzes the final step in the synthesis of phosphatidylcholine via the Kennedy pathway by the transfer of phosphocholine from CDP-choline to 1,2-diacyl-sn-glycerol. The CDP-choline and CDP-ethanolamine pathways are separate routes of phospholipid biosynthesis in mammalian cells, although the CEPT is probably a participant in both pathways. Molecular regulation of the CDP-choline pathway, DNA synthesis and phosphatidylcholine synthesis are not linked, overview. The CDP-choline pathway of phosphatidylcholine synthesis is essential in proliferating cells. The phosphatidylcholine pool is dynamic and the amount of PtdCho represents a balance between synthesis and degradation. phosphatidylcholine and other phospholipids are synthesized in the G2/M phase, rather than S phase. Physiological role of the CDP-choline pathway, overview
metabolism
CPT is a key enzyme in the metabolism of oil in soybean seeds, the enzyme is involved in lipid biosynthesis in soybean seeds and is important for triacylglycerol biosynthesis, together with lysophosphatidylcholine acyltransferase, EC 2.3.1.23. diacylglycerol can also be converted to triacylglycerol by acylation at position 3 of the glycerol molecule in a reaction catalyzed by diacylglycerol acyltransferase, EC 2.3.1.20
metabolism
the CDP-choline and CDP-ethanolamine pathways are separate routes of phospholipid biosynthesis in mammalian cells, although the CEPT is probably a participant in both pathways. The CPT activity responsible for the synthesis of platelet-activating factor (PAF) is different from those responsible for PtdCho synthesis on the basis of the enzyme's sensitivity to dithiothreitol. Molecular regulation of the CDP-choline pathway, overview. The CDP-choline pathway of phosphatidylcholine synthesis is essential in proliferating cells. The phosphatidylcholine pool is dynamic and the amount of PtdCho represents a balance between synthesis and degradation. Physiological role of the CDP-choline pathway, overview
physiological function
cholinephosphotransferase is involved in glycoglycerophospholipid biosynthesis
physiological function
-
cholinephosphotransferase is the terminal enzyme for the de novo biosynthesis of phosphatidylcholine
physiological function
-
PDCT is required for the efficient metabolism of engineered hydroxy fatty acids in Arabidopsis thaliana seeds
physiological function
the enzyme produces membrane lipids by reversibly converting diacylglycerol into phosphatidylcholine, which is a substrate for polyunsaturated fatty acid biosynthesis and can replenish the pool of acyl-CoA through the action of cytoplasmic lysophosphatidylcholine acyltransferase
physiological function
CEPT1 is important for phosphatidylethanolamine formation from fatty acids such as 32:2, 32:1, 34:2, and 34:1, i.e. reaction of EC 2.7.8.1. Brefeldin A treatment does not significantly affect the levels of the different phosphatidylethanolamine species. CEPT1 greatly prefers diacylglycerols 16:0-18:1 to other acceptors
physiological function
endothelial cells of mice carrying a conditional endothelial cell-specific deletion of Cept1 demonstrate decreased proliferation, migration, and tubule formation, and mice carrying the conditional deletion have reduced perfusion and angiogenesis in ischemic hind-limbs. Peripheral ischemic recovery and PPARalpha signaling is further compromised by Streptozotocin-induced diabetes, and ameliorated by feeding fenofibrate
physiological function
expression of Cpt complements a Saccharomyces cerevisiae CPT1 mutant, and expression of the entire Treponema denticola LicCA-Cpt pathway in Escherichia coli results in phosphatidylcholine biosynthesis
physiological function
isoforms AAPT1 and AAPT2 contribute to phosphatidylcholine and phosphatidylethanolamine synthesis and exhibit choline/ethanolamine phosphotransferase-like enzymatic properties. The overexpression of AAPT1 and AAPT2 in Arabidopsis leads to reduced levels of seed triacylglycerol and polyunsaturated fatty acids and decreases seed germination under freezing stress
physiological function
-
cholinephosphotransferase is involved in glycoglycerophospholipid biosynthesis
-
physiological function
-
expression of Cpt complements a Saccharomyces cerevisiae CPT1 mutant, and expression of the entire Treponema denticola LicCA-Cpt pathway in Escherichia coli results in phosphatidylcholine biosynthesis
-
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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). CHPT1_BOVIN
406
6
45249
Swiss-Prot
Mitochondrion (Reliability: 4)
CHPT1_CHICK
335
7
37091
Swiss-Prot
Mitochondrion (Reliability: 5)
CHPT1_DANRE
382
8
42463
Swiss-Prot
other Location (Reliability: 4)
CHPT1_HUMAN
406
8
45097
Swiss-Prot
Mitochondrion (Reliability: 3)
CHPT1_MOUSE
398
8
44608
Swiss-Prot
Mitochondrion (Reliability: 4)
CHPT1_RAT
398
8
44601
Swiss-Prot
Mitochondrion (Reliability: 4)
CHPT1_XENLA
402
8
44513
Swiss-Prot
other Location (Reliability: 3)
EPT1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
391
7
44560
Swiss-Prot
other Location (Reliability: 2)
CEPT1_CHICK
416
8
46097
Swiss-Prot
Mitochondrion (Reliability: 4)
CEPT1_HUMAN
416
8
46554
Swiss-Prot
Mitochondrion (Reliability: 5)
CEPT1_MOUSE
416
8
46434
Swiss-Prot
other Location (Reliability: 5)
CEPT1_RAT
416
8
46498
Swiss-Prot
other Location (Reliability: 5)
CEPT1_XENLA
416
8
46637
Swiss-Prot
Mitochondrion (Reliability: 4)
CEPT1_XENTR
416
8
46606
Swiss-Prot
Mitochondrion (Reliability: 5)
AAPT1_ARATH
389
8
43542
Swiss-Prot
Mitochondrion (Reliability: 5)
AAPT2_ARATH
389
7
43639
Swiss-Prot
other Location (Reliability: 3)
CPT1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
393
8
44829
Swiss-Prot
Mitochondrion (Reliability: 4)
A0A061INC6_CRIGR
430
8
48028
TrEMBL
other Location (Reliability: 5)
Q4Q0H0_LEIMA
417
6
46344
TrEMBL
other Location (Reliability: 3)
A0A060RQA2_PLARE
391
8
45087
TrEMBL
other Location (Reliability: 5)
A0A6G5QIV4_9PROT
273
0
32828
TrEMBL
-
B7PMX3_IXOSC
395
7
43208
TrEMBL
Mitochondrion (Reliability: 4)
A0A0Y9XW56_PLABE
390
10
44521
TrEMBL
other Location (Reliability: 4)
A1Z9E0_DROME
417
6
46008
TrEMBL
Mitochondrion (Reliability: 5)
A0A6J8BRF2_MYTCO
377
8
42234
TrEMBL
other Location (Reliability: 4)
A0A077Y863_PLAYE
390
9
44740
TrEMBL
other Location (Reliability: 5)
A0A564ZZF4_PLAVI
390
8
44924
TrEMBL
other Location (Reliability: 5)
A0A1S6U9J7_9PROT
272
0
32827
TrEMBL
-
L7JU83_TRAHO
378
8
43441
TrEMBL
other Location (Reliability: 3)
A0A1S6TR38_9PROT
275
0
33410
TrEMBL
-
A1Z9D9_DROME
417
8
46379
TrEMBL
Mitochondrion (Reliability: 5)
A0A0B4KFL2_DROME
373
6
41614
TrEMBL
Mitochondrion (Reliability: 5)
A0A061IP82_CRIGR
342
6
38326
TrEMBL
other Location (Reliability: 5)
A0A812AVW1_SEPPH
394
8
44801
TrEMBL
other Location (Reliability: 5)
W8T4E8_PEPAC
349
11
37258
TrEMBL
-
A0A7C8ZD89_OPUST
286
4
31773
TrEMBL
other Location (Reliability: 2)
A4IE03_LEIIN
417
6
46359
TrEMBL
other Location (Reliability: 3)
G3IBU9_CRIGR
416
8
46538
TrEMBL
other Location (Reliability: 5)
K4LCK2_THEPS
Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB)
354
11
36771
TrEMBL
-
B9RLB3_RICCO
441
6
49837
TrEMBL
other Location (Reliability: 4)
Q6U9W9_CHLRE
383
8
42399
TrEMBL
other Location (Reliability: 5)
A0A061INB0_CRIGR
344
7
37951
TrEMBL
other Location (Reliability: 5)
A0A7R8H8D8_LEPSM
158
2
17491
TrEMBL
other Location (Reliability: 3)
A0A812CXQ2_SEPPH
376
9
43119
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B4K7Y4_DROME
417
8
46369
TrEMBL
Mitochondrion (Reliability: 5)
A0A1G4GZT3_PLAVI
390
8
44890
TrEMBL
Mitochondrion (Reliability: 5)
A0A088S3D0_9TRYP
417
9
46725
TrEMBL
other Location (Reliability: 4)
A0A061IQG2_CRIGR
386
8
42888
TrEMBL
other Location (Reliability: 5)
A4HQA8_LEIBR
417
9
46729
TrEMBL
other Location (Reliability: 4)
Q7TT48_CAVPO
195
3
21733
TrEMBL
Secretory Pathway (Reliability: 2)
G0QLB3_ICHMG
Ichthyophthirius multifiliis (strain G5)
611
12
69866
TrEMBL
other Location (Reliability: 4)
A0A1G4IGI1_TRYEQ
432
8
47942
TrEMBL
Mitochondrion (Reliability: 4)
A0A1Z5JGT8_FISSO
434
6
48475
TrEMBL
other Location (Reliability: 2)
A0A8J5EPM9_9ASCO
393
8
44021
TrEMBL
other Location (Reliability: 4)
C3PKS0_CORA7
Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 / CN-1)
253
2
26730
TrEMBL
-
A0A8J5BFI7_9ASCO
393
8
44046
TrEMBL
other Location (Reliability: 4)
C6KTB9_PLAF7
391
8
45082
TrEMBL
other Location (Reliability: 5)
B5DEU1_XENTR
389
8
43247
TrEMBL
other Location (Reliability: 4)
B7PTD6_IXOSC
371
8
41842
TrEMBL
other Location (Reliability: 3)
E0VXP8_PEDHC
427
7
48213
TrEMBL
other Location (Reliability: 5)
K0KHU0_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
291
7
32815
TrEMBL
other Location (Reliability: 2)
G8SFH8_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
251
3
26248
TrEMBL
-
A0A1Z5K1U1_FISSO
436
8
48537
TrEMBL
other Location (Reliability: 3)
Q73RR4_TREDE
Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)
333
0
38502
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46500
-
x * 46500, hCEPT1, SDS-PAGE and deduced from gene sequence, seven membrane-spanning helices
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 46500, hCEPT1, SDS-PAGE and deduced from gene sequence, seven membrane-spanning helices
additional information
-
integral membrane-bound protein, overview on structure and properties
additional information
the enzyme contains domains for a CDP-alcohol phosphatidyltransferase, choline/ethanolamine phosphotransferase, and signal peptide and transmembrane regions (nine transmembrane regions in the protein encoded by Glyma12g08720 and eight transmembrane regions in the protein encoded by Glyma02g14210)
additional information
-
the enzyme contains domains for a CDP-alcohol phosphatidyltransferase, choline/ethanolamine phosphotransferase, and signal peptide and transmembrane regions (nine transmembrane regions in the protein encoded by Glyma12g08720 and eight transmembrane regions in the protein encoded by Glyma02g14210)
additional information
-
integral membrane-bound protein, overview on structure and properties
additional information
-
integral membrane-bound protein, overview on structure and properties
additional information
-
integral membrane-bound protein, overview on structure and properties
additional information
-
integral membrane-bound protein, overview on structure and properties
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
transgenic lines expressing RNA interference (RNAi) targeting either single or double genes show significant changes in the fatty acid composition of seed oil, i.e. an increase in oleic acid (18:1) in all transgenic lines, and a cumulative effect of increased 18:1 in the LPCAT-PDCT double-gene RNAi. PDCT single-gene RNAi has no obvious effect on the level of 22:1 fatty acid
additional information
-
chimeric constructs of cholinephosphotransferase and choline/ethanolaminephosphotransferase, structure-function analysis of segments
additional information
-
chimeric constructs of cholinephosphotransferase and choline/ethanolaminephosphotransferase, study on mechanism of cation activation
additional information
-
chimeric constructs of cholinephosphotransferase and choline/ethanolaminephosphotransferase, study on enzyme regulation
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
55
-
1 min, 90% loss of activity, whole microsomes, less than 60% loss of activity, partially purified enzyme
60
-
20 min heating results in total loss of activity, microsomal fraction of human mesangial cells (HMC)
50
-
20 min heating results in loss of 80% of activity, microsomal fraction of human mesangial cells (HMC)
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing the microsomal preparation 5times destroys activity by 50%
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
overview: purification
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CG7149, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression from vector mammalian expression vector pcDNA3.1/V5-His-TOPO in HeLa cells and in Drosophila S2 cells
gene GLYMA_12G0819001, DNA and amino acid sequence determination, analysis, and comparison, gene modeling using sequences Glyma02g14210 and Glyma12g08720, the soybean genome possesses two loci encoding the enzyme CPT, overview. Presence of binding sites for DNA-binding with one finger proteins in promoter regions of the gene model encoding CPT
gene PDCT1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, the gene sequences of isozymes LuPDCT1 and LuPDCT2 show very high nucleotide sequence identity of 97%, functional complementation of the enzyme-deficient rod1 mutant of Arabidopsis thaliana by expression of the seed-speficic isozymes, restoring polyunsaturated fatty acid levels (16.4% and 19.7% increases in C18-PUFAs, respectively, with a concomitant decrease in the proportion of oleic acid). Functional coexpression of the isozymes with fatty acid desaturases FAD2 and FAD3 in Saccharomyces cerevisiae leads to increased polyunsaturated fatty acid levels
gene PDCT2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, the gene sequences of isozymes LuPDCT1 and LuPDCT2 show very high nucleotide sequence identity of 97%, functional complementation of the enzyme-deficient rod1 mutant of Arabidopsis thaliana by expression of the seed-speficic isozymes, restoring polyunsaturated fatty acid levels (16.4% and 19.7% increases in C18-PUFAs, respectively, with a concomitant decrease in the proportion of oleic acid). Functional coexpression of the isozymes with fatty acid desaturases FAD2 and FAD3 in Saccharomyces cerevisiae leads to increased polyunsaturated fatty acid levels
genes PDCT1 and PDCT2, DNA and amino acid sequence determination and analysis, sequence comparisons
-
into the vectors pCRBluntII, pENTR/D-TOPO and pDEST14, finally the pDEST14 construct is used for the expression of the protein in Escherichia coli BL21-AI cells
overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cholinephosphotransferase activity and its expression are significantly higher in breast cancer tissues
-
expression of PiCPT1 is upregulated in Phytophthora infestans organisms fed with exogenous very long-chain polyunsaturated fatty acids
-
expression of the gene encoding CPT, but not CEPT, EC 2.7.8.1, increases during lipopolysaccahride-induced endoplasmic reticulum biogenesis in B-lymphocytes
gene cis-elements respond to biotic and abiotic stress, the enzyme is expressed under conditions of water or salinity stress, during infection with pathogens, in response to salicylic acid signaling, during somatic embryo differentiation, in immature seeds, in root tissues, and in soybean calli grown in the dark
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
since CPT expression is associated with elaboration of new endoplasmic reticulum membrane, it may be useful as a marker protein for endoplasmic reticulum expansion
biotechnology
medicine
synthesis
heterologous expression in Camelina sativa of lychee phosphatidylcholine diacylglycerol cholinephosphotransferase PDCT. Camelina lines coexpressing PDCT and Escherichia coli cyclopropane synthase CPS show up to a 50% increase of cyclopropane fatty acids in mature seed, relative to the CPS background. The expression of PDCT strongly reduces the level of C18:1 substrate at phosphatidylcholine sn-1 and phosphatidylcholine sn-2 (i.e. the sites of cyclopropane fatty acids synthesis), while the levels of cyclopropane fatty acids increased in phosphatidylcholine sn-2, diacylglycerol sn-1 and diacylglycerol sn-2, and both sn-1/3 and sn-2 positions in triacylglycerol
biotechnology
-
targeting of unusual fatty acids to triacylglycerol synthesis and their exclusion from membrane lipids are not achieved on the basis of the diacylglycerol substrate specificities of enzyme
biotechnology
-
targeting of unusual fatty acids to triacylglycerol synthesis and their exclusion from membrane lipids are not achieved on the basis of the diacylglycerol substrate specificities of enzyme
biotechnology
-
targeting of unusual fatty acids to triacylglycerol synthesis and their exclusion from membrane lipids are not achieved on the basis of the diacylglycerol substrate specificities of enzyme
biotechnology
-
targeting of unusual fatty acids to triacylglycerol synthesis and their exclusion from membrane lipids are not achieved on the basis of the diacylglycerol substrate specificities of enzyme
medicine
-
exposure of cortical neurons to neurotoxic concentrations of N-methyl-D-aspartate strongly reduces enzymic activity
medicine
-
cholinephosphotransferase can be used as a biomarker for breast cancer in an animal model
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Banas, A.; Dahlqvist, A.; Stahl, U.; Lenman, M.; Stymne, S.
The involvement of phospholipid:diacylglycerol acyltransferases in triacylglycerol production
Biochem. Soc. Trans.
28
703-705
2000
Ricinus communis, Crepis palaestina, Crepis rubra
brenda
Gasull, T.; Sarri, E.; DeGregorio-Rocasolano, N.; Trullas, R.
NMDA receptor overactivation inhibits phospholipid synthesis by decreasing choline-ethanolamine phosphotransferase activity
J. Neurosci.
23
4100-4107
2003
Rattus norvegicus
brenda
Lee, T.C.; Blank, M.L.; Fitzgerald, V.; Snyder, F.
Formation of alkylacyl- and diacylglycerophosphocholines via diradylglycerol cholinephosphotransferase in rat liver
Biochim. Biophys. Acta
713
479-483
1982
Rattus norvegicus
brenda
Coleman, R.; Bell, R.M.
Phospholipid synthesis in isolated fat cells. Studies of microsomal diacylglycerol cholinephosphotransferase and diacylglycerol ethanolaminephosphotransferase activities
J. Biol. Chem.
252
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1977
Rattus norvegicus
brenda
Renooij, W.; Snyder, F.
Biosynthesis of 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet activating factor and a hypotensive lipid) by cholinephosphotransferase in various rat tissues
Biochim. Biophys. Acta
663
545-556
1981
Rattus norvegicus
brenda
Ghosh, S.; Oten, P.W.; Mukherjee, S.; Das, S.K.
Study of properties of cholinephosphotransferase from fetal guinea pig lung mitochondria and microsomes
Mol. Cell. Biochem.
101
157-166
1991
Cavia porcellus
brenda
Wilson, A.C.; Barran, L.R.
Study of the properties of choline phoshotransferase from fetal guinea pig lung mitochondria and microsomes
Trans. Br. Mycol. Soc.
85
141-144
1985
Fusarium oxysporum
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brenda
Parthasarathy, S.; Cady, R.K.; Kraushaar, D.S.; Sladek, N.E.; Bauman, W.J.
Inhibition of diacylglycerol:CDPcholine cholinephosphotransferase activity by dimethylaminoethyl p-chlorophenoxyacetate
Lipids
13
161-164
1978
Rattus norvegicus
brenda
Lee, T.C.; Snyder, F.
1-Alkyl-2-acetyl-sn-glycerol cholinephosphotransferase
Methods Enzymol.
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Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
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Cholinephosphotransferase from mammalian sources
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Rattus norvegicus
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Lianos, E.A.; Zanglis, A.
Biosynthesis and metabolism of 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine in rat glomerular mesangial cells
J. Biol. Chem.
262
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1987
Rattus norvegicus
brenda
Woodard, D.S.; Lee, T.c.; Snyder, F.
The final step in the de novo biosynthesis of platelet-activating factor. Properties of a unique CDP-choline:1-alkyl-2-acetyl-sn-glycerol choline-phosphotransferase in microsomes from the renal inner medulla of rats
J. Biol. Chem.
262
2520-2527
1987
Rattus norvegicus
brenda
Heller, R.; Bussolino, F.; Ghigo, D.; Garbarino, G.; Pescarmona, G.; Till, U.; Bosia, A.
Stimulation of platelet-activating factor synthesis in human endothelial cells by activation of the de novo pathway. Phorbol 12-myristate 13-acetate activates 1-alkyl-2-lyso-sn-glycero-3-phosphate:acetyl-CoA acetyltransferase and dithiothreitol-insensitive 1-alkyl-2-acetyl-sn-glycerol:CDP-choline cholinephosphotransferase
J. Biol. Chem.
266
21358-21361
1991
Homo sapiens
brenda
Tsoukatos, D.C.; Tselepis, A.D.; Lekka, M.E.
Studies on the subcellular distribution of 1-O-alkyl-2-acetyl-sn-glycero phosphocholine (PAF) and on the enzymic activities involved in its biosynthesis within the ciliate Tetrahymena pyriformis
Biochim. Biophys. Acta
1170
258-264
1993
Tetrahymena pyriformis
brenda
Ishidate, K.; Matsuo, R.; Nakazawa, Y.
CDPcholine:1,2-diacylglycerol cholinephosphotransferase from rat liver microsomes. I. Solubilization and characterization of the partially purified enzyme and the possible existence of an endogenous inhibitor
Lipids
28
89-96
1993
Rattus norvegicus
brenda
O, K.; Choy, P.C.
Solubilization and partial purification of cholinephosphotransferase in hamster tissues
Lipids
25
122-124
1990
Mesocricetus auratus
brenda
Mantel, C.R.; Schulz, A.R.; Miyazawa, K.; Broxmeyer, H.E.
Kinetic selectivity of cholinephosphotransferase in mouse liver: the Km for CDP-choline depends on diacylglycerol structure
Biochem. J.
289
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1993
Mus musculus
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brenda
Bru, R.; Blchliger, E.; Luisi, P.L.
sn-1,2-Diacylglycerol cholinephosphotransferase from pig liver: mixed micellar assay and kinetic analysis of the partially pure enzyme
Arch. Biochem. Biophys.
307
295-303
1993
Sus scrofa
brenda
Goracci, G.; Francescangeli, E.; Horrocks, L.A.; Porcellati, G.
The reverse reaction of cholinephosphotransferase in rat brain microsomes. A new pathway for degradation of phosphatidylcholine
Biochim. Biophys. Acta
664
373-379
1981
Rattus norvegicus
brenda
Pontoni, G.; Manna, C.; Salluzzo, A.; Del Piano, L.; Gallett, P.; De Rosa, M.; Zappia, V.
Studies on enzyme-substrate interactions of cholinephosphotransferase from rat liver
Biochim. Biophys. Acta
836
222-232
1985
Rattus norvegicus
brenda
Cornell, R.; MaxLennan, D.H.
Solubilization and reconstitution of cholinephosphotransferase from sarcoplasmic reticulum: stabilization of solubilized enzyme by diacylglycerol and glycerol
Biochim. Biophys. Acta
821
97-105
1985
Oryctolagus cuniculus
brenda
Wang, P.; Dechatelet, L.R.; Waite, M.
Enzymes of phospholipid synthesis in Bacillus Calmette-Guerin induced rabbit alveolar macrophage. Characterization and localization of cytidine diphosphocholine phosphotransferase and monoacylphospholipid acyltransferase
Biochim. Biophys. Acta
450
311-321
1976
Oryctolagus cuniculus
brenda
Baker, R.R.; Chang, H.Y.
Cholinephosphotransferase activities in microsomes and neuronal nuclei isolated from immature rabbit cerebral cortex: the use of endogenously generated diacylglycerols as substrate
Can. J. Biochem.
60
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1982
Oryctolagus cuniculus
brenda
Kanoh, H.; Ohno, K.
1,2-Diacylglycerol: CDPcholine cholinephosphotransferase
Methods Enzymol.
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536-546
1981
Rattus norvegicus
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Dorman, R.V.; Bischoff, S.B.; Terrian, D.M.
Choline and ethanolamine phosphotransferase activities in glomerular particles isolated from bovine cerebellar cortex
Neurochem. Res.
11
1167-1179
1986
Bos taurus
brenda
Binaglia, L.; Roberti, R.; Vecchini, A.; De Meo, G.; Porcellati, G.
Temperature-dependence of choline phosphotransferase and ethanolamine phosphotransferase in rat brain microsomes
Ital. J. Biochem.
29
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1980
Rattus norvegicus
brenda
Sribney, M.; Lyman, E.M.
Stimulation of phosphorylcholine-glyceride transferase activity by unsaturated fatty acids
Can. J. Biochem.
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1973
Gallus gallus
brenda
Hjelmstad, R.H.; Bell, R.M.
Choline- and ethanolaminephosphotransferases from Saccharomyces cerevisiae
Methods Enzymol.
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1992
Saccharomyces cerevisiae
brenda
Justin, A.M.; Demandre, C.; Tremolieres, A.; Mazliak, P.
No discrimination by choline- and ethanolamine phosphotransferases from potato tuber microsomes in molecular species of endogenous diacylglycerols
Biochim. Biophys. Acta
836
1-7
1985
Solanum tuberosum
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brenda
Goracci, G.; Francescangeli, E.; Horrocks, L.A.; Porcellati, G.
A comparison of the reversibility of phosphoethanolamine transferase and phosphocholine transferase in rat brain microsomes
Biochim. Biophys. Acta
876
387-391
1986
Rattus norvegicus
brenda
Taniguchi, S.; Morikawa, S.; Hayashi, H.; Fujii, K.; Mori, H.; Fujiwara, M.; Fujiwara, M.
Effects of Ca2+ on ethanolaminephosphotransferase and cholinephosphotransferase in rabbit platelets
J. Biochem.
100
485-491
1986
Oryctolagus cuniculus
brenda
Justin, A.M.; Demandre, C.; Mazliak, P.
Choline- and ethanolaminephosphotransferases from pea leaf and soya beans discriminate 1-palmitoyl-2-linoleoyldiacylglycerol as preferred substrate
Biochim. Biophys. Acta
922
364-371
1987
Glycine max, Pisum sativum
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brenda
Smith, J.D.
Differential selectivity of cholinephosphotransferase and ethanolaminephosphotransferase of Tetrahymena for diacylglycerol and alkylacylglycerol
J. Biol. Chem.
260
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1985
Tetrahymena thermophila
brenda
Hjelmstad, R.H.; Bell, R.M.
sn-1,2-Diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Mixed micellar analysis of the CPT1 and EPT1 gene products
J. Biol. Chem.
266
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1991
Saccharomyces cerevisiae
brenda
O, K.M.; Siow, Y.L.; Choy, P.C.
Hamster liver cholinephosphotransferase and ethanolaminephosphotransferase are separate enzymes
Biochem. Cell Biol.
67
680-686
1989
Mesocricetus auratus
brenda
Roberti, R.; Mancini, A.; Freysz, L.; Binaglia, L.
Reversibility of the reactions catalyzed by cholinephosphotransferase and ethanolaminephosphotransferase solubilized from rat-brain microsomes
Biochim. Biophys. Acta
1165
183-188
1992
Rattus norvegicus
brenda
Kanoh, H.; Ohno, K.
Utilization of endogenous phospholipids by the backreaction of CDP-choline (-ethanolamine): 1,2-diglyceride choline (ethanolamine)-phosphotransferase in rat liver microsomes
Biochim. Biophys. Acta
306
203-217
1973
Rattus norvegicus
brenda
Kanoh, H.; Ohno, K.
Substrate-selectivity of rat liver microsomal 1,2-diacylglycerol: CDP-choline(ethanolamine) choline(ethanolamine)phosphotransferase in utilizing endogenous substrates
Biochim. Biophys. Acta
380
199-207
1975
Rattus norvegicus
brenda
Morimoto, K.; Kanoh, H.
Effect of phospholipase A2 on rat liver microsomal diacylglycerol cholinephosphotransferase, diacylglycerol ethanolaminephosphotransferase and diacylglycerol acyltransferase
Biochim. Biophys. Acta
531
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1978
Rattus norvegicus
brenda
Freysz, L.; Horrocks, L.A.; Mandel, P.
Effects of deoxycholate and phospholipase A2 on choline and ethanolamine phosphotransferases of chicken brain microsomes
Biochim. Biophys. Acta
489
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1977
Gallus gallus
brenda
Strosznajder, J.; Radominska-Pyrek, A.; Horrocks, L.A.
Choline and ethanolamine glycerophospholipid synthesis in isolated synaptosomes of rat brain
Biochim. Biophys. Acta
574
48-56
1979
Rattus norvegicus
brenda
Percy, A.K.; Carson, M.A.; Moore, J.F.; Waechter, C.J.
Control of phosphatidylethanolamine metabolism in yeast: diacylglycerol ethanolaminephosphotransferase and diacylglycerol cholinephosphotransferase are separate enzymes
Arch. Biochem. Biophys.
230
69-81
1984
Saccharomyces cerevisiae
brenda
Morimoto, K.; Kanoh, H.
Acyl chain length dependency of diacylglycerol cholinephosphotransferase and diacylglycerol ethanolaminephosphotransferase. Effect of different saturated fatty acids at the C-1 or C-2 position of diacylglycerol on solubilized rat liver microsomal enzymes
J. Biol. Chem.
253
5056-5060
1978
Rattus norvegicus
brenda
Kanoh, H.; Ohno, K.
Solubilization and purification of rat liver microsomal 1,2-diacylglycerol: CDP-choline cholinephosphotransferase and 1,2-diacylglycerol: CDP-ethanolamine ethanolaminephosphotransferase
Eur. J. Biochem.
66
201-210
1976
Rattus norvegicus
brenda
Holub, B.J.
Differential utilization of 1-palmitoyl and 1-stearoyl homologues of various unsaturated 1,2-diacyl-sn-glycerols for phosphatidylcholine and phosphatidylethanolamine synthesis in rat liver microsomes
J. Biol. Chem.
253
691-696
1978
Rattus norvegicus
brenda
Goode, J.H.; Dewey, R.E.
Characterization of aminoalcoholphosphotransferases from Arabidopsis thaliana and soybean
Plant Physiol. Biochem.
37
445-457
1999
Glycine max, Arabidopsis thaliana (O82567)
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brenda
Henneberry, A.L.; McMaster, C.R.
Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine
Biochem. J.
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1999
Homo sapiens
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brenda
Hjelmstad, R.H.; Morash, S.C.; McMaster, C.R.; Bell, R.M.
Chimeric enzymes. Structure-function analysis of segments of sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases
J. Biol. Chem.
269
20995-21002
1994
Saccharomyces cerevisiae
brenda
McMaster, C.R.; Morash, S.C.; Bell, R.M.
Phospholipid and cation activation of chimaeric choline/ethanolamine phosphotransferases
Biochem. J.
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1996
Saccharomyces cerevisiae
brenda
McMaster, C.R.; Bell, R.M.
Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases
J. Biol. Chem.
269
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Saccharomyces cerevisiae
brenda
McMaster, C.R.; Bell, R.M.
CDP-choline:1,2-diacylglycerol cholinephosphotransferase
Biochim. Biophys. Acta
1348
100-110
1997
Saccharomyces cerevisiae, Glycine max, Homo sapiens, Mesocricetus auratus, Rattus norvegicus
brenda
Vogel, G.; Browse, J.
Cholinephosphotransferase and diacylglycerol acyltransferase. Substrate specificities at a key branch point in seed lipid metabolism
Plant Physiol.
110
923-931
1996
Brassica napus, Carthamus tinctorius, Cuphea lanceolata, Ricinus communis
brenda
Fernandez-Tome, M. del C.; Speziale, E.H.; Sterin-Speziale, N.B.
Phospholipase C inhibitors and prostaglandins differentially regulate phosphatidylcholine synthesis in rat renal papilla. Evidence of compartmental regulation of CTP:phosphocholine cytidylyltransferase and CDP-choline:1,2-diacylglycerol cholinephosphotransferase
Biochim. Biophys. Acta
1583
185-194
2002
Rattus norvegicus
brenda
Carrasco, M.P.; Segovia, J.L.; Marco, C.
Modulation of biosynthesis of phosphatidylcholine via CDP-choline in rat liver: influence of ethanol on the microsomal cholinephosphotransferase activity
Mol. Cell. Biochem.
217
43-50
2001
Rattus norvegicus
brenda
Wright, M.M.; McMaster, C.R.
PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1)
Lipids
37
663-672
2002
Homo sapiens
brenda
Kudolo, G.B.; Harper, M.J.
Lyso-PAF:acetyl-CoA acetyltransferase and CDP-choline cholinephosphotransferase activities in the rabbit endometrium
J. Lipid Mediat. Cell Signal.
11
145-158
1995
Oryctolagus cuniculus
brenda
Chatterjee, D.; Mukherjee, S.; Das, S.K.
Regulation of cholinephosphotransferase by thyroid hormone
Biochem. Biophys. Res. Commun.
282
861-864
2001
Cavia porcellus
brenda
Henneberry, A.L.; Wistow, G.; McMaster, C.R.
Cloning, genomic organization, and characterization of a human cholinephosphotransferase
J. Biol. Chem.
275
29808-29815
2000
Homo sapiens (Q8WUD6), Homo sapiens
brenda
Oxley, A.; Torstensen, B.E.; Rustan, A.C.; Olsen, R.E.
Enzyme activities of intestinal triacylglycerol and phosphatidylcholine biosynthesis in Atlantic salmon (Salmo salar L.)
Comp. Biochem. Physiol. B
141
77-87
2005
Salmo salar
brenda
Roy, S.S.; Mukherjee, S.; Kabir, S.; Rajaratnam, V.; Smith, M.; Das, S.K.
Inhibition of cholinephosphotransferase activity in lung injury induced by 2-chloroethyl ethyl sulfide, a mustard analog
J. Biochem. Mol. Toxicol.
19
289-297
2005
Cavia porcellus
brenda
Kim, K.S.; Park, J.H.; Cho, S.H.
Cloning and expression of a cDNA AAPT3 encoding aminoalcoholphosphotransferase isoform from Chinese cabbage
Korean J. Biol. Sci.
8
105-109
2004
Brassica rapa (Q8W1E9)
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brenda
Gohda, T.; Tanimoto, M.; Shiina, K.; Ito, T.; Kobayashi, M.; Hagiwara, S.; Kaneko, S.; Makita, Y.; Funabiki, K.; Horikoshi, S.; Tomino, Y.
Altered mouse cholinephosphotransferase gene expression in kidneys of type 2 diabetic KK/TA mouse
Metabolism
53
842-846
2004
Mus musculus
brenda
Roy, S.S.; Mukherjee, S.; Mukhopadhyay, S.; Das, S.K.
Differential effect of cadmium on cholinephosphotransferase activity in normal and cancerous human mammary epithelial cell lines
Mol. Cancer Ther.
3
199-204
2004
Homo sapiens
brenda
Sriburi, R.; Bommiasamy, H.; Buldak, G.L.; Robbins, G.R.; Frank, M.; Jackowski, S.; Brewer, J.W.
Coordinate regulation of phospholipid biosynthesis and secretory pathway gene expression in XBP-1(S)-induced endoplasmic reticulum biogenesis
J. Biol. Chem.
282
7024-7034
2007
Homo sapiens (Q8WUD6)
brenda
Fagone, P.; Sriburi, R.; Ward-Chapman, C.; Frank, M.; Wang, J.; Gunter, C.; Brewer, J.W.; Jackowski, S.
Phospholipid biosynthesis program underlying membrane expansion during B-lymphocyte differentiation
J. Biol. Chem.
282
7591-7605
2007
Homo sapiens
brenda
Johnston, M.K.; Jacob, N.P.; Brodl, M.R.
Heat shock-induced changes in lipid and protein metabolism in the endoplasmic reticulum of barley aleurone layers
Plant Cell Physiol.
48
31-41
2007
Hordeum vulgare
brenda
Tsoupras, A.B.; Fragopoulou, E.; Nomikos, T.; Iatrou, C.; Antonopoulou, S.; Demopoulos, C.A.
Characterization of the de novo biosynthetic enzyme of platelet activating factor, DDT-insensitive cholinephosphotransferase, of human mesangial cells
Mediators Inflamm.
2007
27683
2007
Homo sapiens
brenda
Ishida, N.; Irikura, D.; Matsuda, K.; Sato, S.; Sone, T.; Tanaka, M.; Asano, K.
Molecular cloning and expression of a novel cholinephosphotransferase involved in glycoglycerophospholipid biosynthesis of Mycoplasma fermentans
Curr. Microbiol.
58
535-540
2009
Mycoplasmopsis fermentans (C4TGF1), Mycoplasmopsis fermentans, Mycoplasmopsis fermentans PG18 (C4TGF1), Mycoplasmopsis fermentans PG18
brenda
Sinha Roy, S.; Mukhopadhyay, S.; Mukherjee, S.; Das, S.K.
Breast cancer is associated with an increase in the activity and expression of cholinephosphotransferase in rats
Life Sci.
83
661-665
2008
Rattus norvegicus
brenda
Chen, Y.; Chi, H.Y.; Meesapyodsuk, D.; Qiu, X.
Phytophthora infestans cholinephosphotransferase with substrate specificity for very-long-chain polyunsaturated fatty acids
Appl. Environ. Microbiol.
79
1573-1579
2013
Phytophthora infestans
brenda
Hu, Z.; Ren, Z.; Lu, C.
The phosphatidylcholine diacylglycerol cholinephosphotransferase is required for efficient hydroxy fatty acid accumulation in transgenic Arabidopsis
Plant Physiol.
158
1944-1954
2012
Arabidopsis thaliana
brenda
Fagone, P.; Jackowski, S.
Phosphatidylcholine and the CDP-choline cycle
Biochim. Biophys. Acta
1831
523-532
2013
Glycine max (I1KH05), Saccharomyces cerevisiae (P17898), Saccharomyces cerevisiae, Homo sapiens (Q8WUD6), Homo sapiens (Q9Y6K0)
brenda
Wickramarathna, A.; Siloto, R.; Mietkiewska, E.; Singer, S.; Pan, X.; Weselake, R.
Heterologous expression of flax phospholipid:diacylglycerol choline phosphotransferase (PDCT) increases polyunsaturated fatty acid content in yeast and Arabidopsis seeds
BMC Biotechnol.
15
63
2015
Linum usitatissimum (A0A0H3U1R3), Linum usitatissimum (A0A0H3U1R4), Linum usitatissimum
brenda
Sousa, C.S.; Barros, B.A.; Barh, D.; Ghosh, P.; Azevedo, V.; Barros, E.G.; Moreira, M.A.
In silico characterization of 1,2-diacylglycerol cholinephosphotransferase and lysophosphatidylcholine acyltransferase genes in Glycine max L. Merrill
Genet. Mol. Res.
15
gmr.15038974
2016
Glycine max (Q39810), Glycine max
brenda
Vacaru, A.M.; van den Dikkenberg, J.; Ternes, P.; Holthuis, J.C.
Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the Golgi lumen
J. Biol. Chem.
288
11520-11530
2013
Drosophila melanogaster (Q8T0S3)
brenda
Guan, R.; Li, X.; Hofvander, P.; Zhou, X.R.; Wang, D.; Stymne, S.; Zhu, L.H.
RNAi targeting putative genes in phosphatidylcholine turnover results in significant change in fatty acid composition in Crambe abyssinica seed oil
Lipids
50
407-416
2015
Crambe hispanica subsp. abyssinica
brenda
Zayed, M.A.; Jin, X.; Yang, C.; Belaygorod, L.; Engel, C.; Desai, K.; Harroun, N.; Saffaf, O.; Patterson, B.W.; Hsu, F.F.; Semenkovich, C.F.
CEPT1-mediated phospholipogenesis regulates endothelial cell function and ischemia-induced angiogenesis through PPARalpha
Diabetes
70
549-561
2020
Mus musculus (Q8BGS7), Homo sapiens (Q9Y6K0), Homo sapiens
brenda
Lager, I.; Jeppson, S.; Gippert, A.; Feussner, I.; Stymne, S.; Marmon, S.
Acyltransferases regulate oil quality in Camelina sativa through both acyl donor and acyl acceptor specificities
Front. Plant Sci.
11
1144
2020
Camelina sativa
brenda
Horibata, Y.; Elpeleg, O.; Eran, A.; Hirabayashi, Y.; Savitzki, D.; Tal, G.; Mandel, H.; Sugimoto, H.
EPT1 (selenoprotein I) is critical for the neural development and maintenance of plasmalogen in humans
J. Lipid Res.
59
1015-1026
2018
Homo sapiens (Q9Y6K0)
brenda
Vences-Guzman, M.A.; Paula Goetting-Minesky, M.; Guan, Z.; Castillo-Ramirez, S.; Cordoba-Castro, L.A.; Lopez-Lara, I.M.; Geiger, O.; Sohlenkamp, C.; Christopher Fenno, J.
1,2-Diacylglycerol choline phosphotransferase catalyzes the final step in the unique Treponema denticola phosphatidylcholine biosynthesis pathway
Mol. Microbiol.
103
896-912
2017
Treponema denticola (Q73RR4), Treponema denticola, Treponema denticola DSM 14222 (Q73RR4)
brenda
Yu, X.H.; Cai, Y.; Chai, J.; Schwender, J.; Shanklin, J.
Expression of a lychee phoshatidylcholine diacylglycerol cholinephosphotransferase with an Escherichia coli cyclopropane synthase enhances cyclopropane fatty acid accumulation in camelina seeds
Plant Physiol.
180
1351-1361
2019
Litchi chinensis (A0A2R2WT05), Litchi chinensis
brenda
Bai, Y.; Zhu, X.; Guo, X.; Zhang, W.; Zhang, G.; Chen, H.; Zhang, Q.
Molecular cloning and functional characterization of GmAAPTs from soybean (Glycine max)
Plant Signal. Behav.
16
1845048
2020
Glycine max (K7K808), Glycine max (Q39810), Glycine max
brenda
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