Information on EC 2.3.1.158 - phospholipid:diacylglycerol acyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.3.1.158
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RECOMMENDED NAME
GeneOntology No.
phospholipid:diacylglycerol acyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phospholipid + 1,2-diacyl-sn-glycerol = lysophospholipid + triacylglycerol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
diacylglycerol and triacylglycerol biosynthesis
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Glycerolipid metabolism
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phospholipid remodeling (phosphatidylcholine, yeast)
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SYSTEMATIC NAME
IUBMB Comments
phospholipid:1,2-diacyl-sn-glycerol O-acyltransferase
This enzyme differs from EC 2.3.1.20, diacylglycerol O-acyltransferase, by synthesising triacylglycerol using an acyl-CoA-independent mechanism. The specificity of the enzyme for the acyl group in the phospholipid varies with species, e.g., the enzyme from castor bean (Ricinus communis) preferentially incorporates vernoloyl (12,13-epoxyoctadec-9-enoyl) groups into triacylglycerol, whereas that from the hawk's beard (Crepis palaestina) incorporates both ricinoleoyl (12-hydroxyoctadec-9-enoyl) and vernoloyl groups. The enzyme from the yeast Saccharomyces cerevisiae specifically transfers acyl groups from the sn-2 position of the phospholipid to diacylglycerol, thus forming an sn-1-lysophospholipid.
CAS REGISTRY NUMBER
COMMENTARY hide
288587-47-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
wild type and mutants lacking wax ester synthase/acyl-coenzyme A: DAG acyltransferase DGAT activity
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Manually annotated by BRENDA team
gene pdat
UniProt
Manually annotated by BRENDA team
gene pdat
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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PDAT belongs to the LCAT-like family
malfunction
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artificial microRNA silencing of PDAT alters the membrane lipid composition, reducing the maximum specific growth rate
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-dioleoylphosphatidylcholine + 1,2-diacylglycerol
1-oleoyl-2-lysophosphatidylcholine + triacylglycerol
show the reaction diagram
1,2-dioleoylphosphatidylethanolamine + 1,2-dioleoylglycerol
1-oleoyl-2-lysophosphatidylethanolamine + trioleoylglycerol
show the reaction diagram
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?
dioleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
show the reaction diagram
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?
dioleoylphosphatidylcholine + 1,2-dioleoylglycerol
1-oleoyl-2-lyso-phosphatidylcholine + trioleoylglycerol
show the reaction diagram
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?
dioleoylphosphatidylcholine + 1-ricinoleoylglycerol
1-oleoyl-2-lysophosphatidylcholine + 1-ricinoleoyl-2-oleoyl-glycerol
show the reaction diagram
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-
-
?
dioleoylphosphatidylcholine + 1-vernoloylglycerol
1-oleoyl-2-lysophosphatidylcholine + 1-vernoloyl-2-oleoylglycerol
show the reaction diagram
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?
linolenoyl-phosphatidylcholine + 1,2-dilinolenoylglycerol
lyso-phosphatidylcholine + trilinolenoylglycerol
show the reaction diagram
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?
palmitoyl phospholipid + dioleoylglycerol
1-lysophospholipid + 1-palmitoyl-2,3-dioleoyl-sn-glycerol
show the reaction diagram
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70% less active in mutants lacking the acyl-CoA-independent acyltransferase activity, individual neutral lipids affects the internal structure of lipid particles
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?
phosphatidylcholine + 1,2-diacylglycerol
2-lysophosphatidylcholine + triacylglycerol
show the reaction diagram
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lysophophatidylcholine acyltransferase activity is mainly responsible for the entry of oleate and linoleate into olive callus lipid metabolism, PDAT is involved in triacylglyceride biosynthesis
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?
phosphatidylethanolamine + 1,2-diacylglycerol
2-lysophosphatidylethanolamine + triacylglycerol
show the reaction diagram
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?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
show the reaction diagram
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
show the reaction diagram
phospholipid + 1,2-diacylglycerol
lysophospholipid + triacylglycerol
show the reaction diagram
phospholipid + 1,2-dipalmitoyl-sn-glycerol
lysophospholipid + 3-acyl-1,2-dipalmitoyl-sn-glycerol
show the reaction diagram
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levels of triacylglyceride biosynthesis through the PDAT pathway were comparable in wild type and mutants, lacking of the acyl-coenzyme A: DAG acyltransferase activity has no effect on the PDAT activity, this is the first time that a PDAT activity has been reported for bacteria
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?
rac-1,2-divernoleoylglycerol + 1,3-dioleoyl-sn-glycerol
1-oleoyl-sn-glycerol + rac-1,2-divernoleoyl-3-oleoylglycerol
show the reaction diagram
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?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
show the reaction diagram
sn-1,2-dioleoylglycerol + sn-1,2-dioleoylglycerol
trioleoylglycerol + sn-1-oleoylglycerol
show the reaction diagram
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?
sn-1,2-dioleoylphosphatidylcholine + sn-1,2-dioleoylglycerol
trioleoylglycerol + sn-1-oleoylphosphatidylcholine
show the reaction diagram
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?
sn-1,2-dioleoylphosphatidylcholine + sn-1-oleoylglycerol
? + sn-1-oleoylphosphatidylcholine
show the reaction diagram
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?
sn-1,2-dioleoylphosphatidylcholine + sn-2-oleoylglycerol
? + sn-1-oleoylphosphatidylcholine
show the reaction diagram
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?
sn-1,2-dioleoylphosphatidylethanolamine + sn-1,2-dioleoylglycerol
trioleoylglycerol + 1-oleoylphosphatidylethanolamine
show the reaction diagram
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?
sn-1,3-dioleoylglycerol + sn-1,3-dioleoylglycerol
trioleoylglycerol + sn-1-oleoylglycerol
show the reaction diagram
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?
sn-2-acyl-phosphatidylcholine + 1,2-diacylglycerol
triacylglycerol + glycerophosphocholine
show the reaction diagram
vernoloyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
show the reaction diagram
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
show the reaction diagram
phospholipid + 1,2-diacylglycerol
lysophospholipid + triacylglycerol
show the reaction diagram
Q9FNA9
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?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-linolenic acid
stimulation; stimulation
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00138
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sn-1,2-distearoylphosphatidylethanolamine as substrate using the membrane bound enzyme
0.001399
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sn-1,2-dipalmitoylphosphatidylethanolamine as substrate using the membrane bound enzyme
0.002453
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sn-1,2-dilinolenoylphosphatidylethanolamine as substrate using the membrane bound enzyme
0.002468
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sn-1,2-dioleoylphosphatidylethanolamine as substrate using the membrane bound enzyme
0.002597
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sn-1,2-dilinoleoylphosphatidylethanolamine as substrate using the membrane bound enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.96
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sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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both PDAT1A and PDAT2 are expressed in the developing endosperm, with PDAT2 showing double the transcript levels of PDAT1A. No expression of RcPDAT1B in castor endosperm
Manually annotated by BRENDA team
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vegetative tissue
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67000
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SDS-PAGE, after deglycosylation
76890
x * 76890, calculated
79072
x * 79072, calculated
80000
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SDS-PAGE
95000
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x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
104600
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x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
120000
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x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant full-length enzyme and truncated PDAT lacking the transmembrane domain from Pichia pastoris by affinity chromatography
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the recombinant protein by Ni2+ affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, functional overexpression in Arabidopsis thaliana roots and leaves
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expression in Escherichia coli, expression in Pichia pastoris of a N-terminal deleted version of PDAT, lacking the predicted membrane-spanning region under the control of the methanol inducible alcohol oxidase promoter
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expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae
gene encoding PDAT, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of full-length enzyme and of truncated PDAT lacking the transmembrane domain in Pichia pastoris
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gene pdat or YALI0E16797g, DNA and amino acid sequence determination and analysis. In vivo expression of DGAT1, DGAT2 and PDAT under the heterologous Yarrowia lipolytica YAT promoter results in 598%, 702% and 278% increases in total fatty acid % dry cell weight over the empty vector control
isozyme PDAT2 and PDAT1A, cloning from cDNA library, expression in Arabidopsis thaliana, coexpression of PDAT1A with Ricinus communis hydroxylated fatty acid hydroxylase, RcFAH, in Arabidopsis thaliana causes a reduction of fatty acids by 73% compared to wild-type plants, isozyme PDAT2 is also functional but less active than isozyme PDAT1A, method optimization, phenotypes, overview
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the gene encoding the enzyme is YNR008w, overexpression of the enzyme-encoding gene increases triacylglycerol content in yeast cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Cr-PDAT is transiently upregulated in response to N deprivation. The protein expression achieves the maximum level at 3 h after the onset of N depletion from the culture medium and then gradually decreases during the following 48 h
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
energy production
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the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production
industry
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the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production
molecular biology
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the conversion of a membrane bound lipid metabolizing enzyme into a soluble and active form might be applied to other enzymes with a membrane anchor region.
synthesis
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the enzyme is useful for production of hydroxylated fatty acids and furtheron polyesters, biodiesel, and lubricants in transgenic plants expressing PDAT thereby avoiding the toxicity of castor bean seeds
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