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Information on EC 2.3.1.158 - phospholipid:diacylglycerol acyltransferase
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2.3.1.158 phospholipid:diacylglycerol acyltransferaseIUBMB Comments
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.
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Word Map
- 2.3.1.158
- triacylglycerols
-
dgats
-
acyl-coa:diacylglycerol
-
acyltransferase1
-
presenile
-
acyl-coa-dependent
- monogalactosyldiacylglycerols
-
oleosins
- energy production
- molecular biology
- synthesis
- industry
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase, CHLREDRAFT_184281, CHLREDRAFT_188937, DGTT1, DGTT2, DGTT3, diacylglycerol acyltransferase type 2, PDAT, PDAT1, PDAT1A, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase
PDAT
PDAT1
phospholipid:diacylglycerol acyltransferase
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase
-
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase
-
-
PDAT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phospholipid + 1,2-diacyl-sn-glycerol = lysophospholipid + triacylglycerol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
288587-47-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dioleoylphosphatidylcholine + 1,2-diacylglycerol
1-oleoyl-2-lysophosphatidylcholine + triacylglycerol
1,2-dioleoylphosphatidylethanolamine + 1,2-dioleoylglycerol
1-oleoyl-2-lysophosphatidylethanolamine + trioleoylglycerol
-
-
-
?
dioleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
dioleoylphosphatidylcholine + 1,2-dioleoylglycerol
1-oleoyl-2-lyso-phosphatidylcholine + trioleoylglycerol
-
-
-
?
dioleoylphosphatidylcholine + 1-ricinoleoylglycerol
1-oleoyl-2-lysophosphatidylcholine + 1-ricinoleoyl-2-oleoyl-glycerol
-
-
-
?
dioleoylphosphatidylcholine + 1-vernoloylglycerol
1-oleoyl-2-lysophosphatidylcholine + 1-vernoloyl-2-oleoylglycerol
-
-
-
?
linolenoyl-phosphatidylcholine + 1,2-dilinolenoylglycerol
lyso-phosphatidylcholine + trilinolenoylglycerol
-
-
-
?
palmitoyl phospholipid + dioleoylglycerol
1-lysophospholipid + 1-palmitoyl-2,3-dioleoyl-sn-glycerol
-
70% less active in mutants lacking the acyl-CoA-independent acyltransferase activity, individual neutral lipids affects the internal structure of lipid particles
-
-
?
phosphatidylcholine + 1,2-diacylglycerol
2-lysophosphatidylcholine + triacylglycerol
-
lysophophatidylcholine acyltransferase activity is mainly responsible for the entry of oleate and linoleate into olive callus lipid metabolism, PDAT is involved in triacylglyceride biosynthesis
-
-
?
phosphatidylethanolamine + 1,2-diacylglycerol
2-lysophosphatidylethanolamine + triacylglycerol
-
-
-
-
?
phospholipid + 1,2-dipalmitoyl-sn-glycerol
lysophospholipid + 3-acyl-1,2-dipalmitoyl-sn-glycerol
-
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
-
-
?
rac-1,2-divernoleoylglycerol + 1,3-dioleoyl-sn-glycerol
1-oleoyl-sn-glycerol + rac-1,2-divernoleoyl-3-oleoylglycerol
-
-
-
-
?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
sn-1,2-dioleoylglycerol + sn-1,2-dioleoylglycerol
trioleoylglycerol + sn-1-oleoylglycerol
-
-
-
-
?
sn-1,2-dioleoylphosphatidylcholine + sn-1,2-dioleoylglycerol
trioleoylglycerol + sn-1-oleoylphosphatidylcholine
-
-
-
-
?
sn-1,2-dioleoylphosphatidylcholine + sn-1-oleoylglycerol
? + sn-1-oleoylphosphatidylcholine
-
-
-
-
?
sn-1,2-dioleoylphosphatidylcholine + sn-2-oleoylglycerol
? + sn-1-oleoylphosphatidylcholine
-
-
-
-
?
sn-1,2-dioleoylphosphatidylethanolamine + sn-1,2-dioleoylglycerol
trioleoylglycerol + 1-oleoylphosphatidylethanolamine
-
-
-
-
?
sn-1,3-dioleoylglycerol + sn-1,3-dioleoylglycerol
trioleoylglycerol + sn-1-oleoylglycerol
-
-
-
-
?
sn-2-acyl-phosphatidylcholine + 1,2-diacylglycerol
triacylglycerol + glycerophosphocholine
vernoloyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
1,2-dioleoylphosphatidylcholine + 1,2-diacylglycerol
1-oleoyl-2-lysophosphatidylcholine + triacylglycerol
-
-
-
?
1,2-dioleoylphosphatidylcholine + 1,2-diacylglycerol
1-oleoyl-2-lysophosphatidylcholine + triacylglycerol
-
-
-
?
1,2-dioleoylphosphatidylcholine + 1,2-diacylglycerol
1-oleoyl-2-lysophosphatidylcholine + triacylglycerol
-
-
-
?
1,2-dioleoylphosphatidylcholine + 1,2-diacylglycerol
1-oleoyl-2-lysophosphatidylcholine + triacylglycerol
-
-
-
?
1,2-dioleoylphosphatidylcholine + 1,2-diacylglycerol
1-oleoyl-2-lysophosphatidylcholine + triacylglycerol
-
-
-
?
1,2-dioleoylphosphatidylcholine + 1,2-diacylglycerol
1-oleoyl-2-lysophosphatidylcholine + triacylglycerol
-
-
-
?
1,2-dioleoylphosphatidylcholine + 1,2-diacylglycerol
1-oleoyl-2-lysophosphatidylcholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
-
PDAT uses membrane lipids (e.g., phospholipids and glycolipids) as the substrates for the acyl transfer reaction or hydrolysis in vivo
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
-
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
the enzyme plays a major role in removing ricinoleic acid and vernolic acid from phospholipids in seeds
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
the enzyme plays a major role in removing ricinoleic acid and vernolic acid from phospholipids in seeds
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
lysophospholipid + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
lysophospholipid + triacylglycerol
enzyme accepts acyl groups ranging from C10 to C22, activity is highly dependent on the acyl composition preferring acyl groups with several double bonds, epoxy, or hydroxy groups, enzyme has a 3fold preference for the sn-2 compared to sn-1 position of phosphatidylcholine, overview
-
-
?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
ricinoleoyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
sn-2-acyl-phosphatidylcholine + 1,2-diacylglycerol
triacylglycerol + glycerophosphocholine
-
-
-
?
sn-2-acyl-phosphatidylcholine + 1,2-diacylglycerol
triacylglycerol + glycerophosphocholine
-
-
-
?
sn-2-acyl-phosphatidylcholine + 1,2-diacylglycerol
triacylglycerol + glycerophosphocholine
-
-
-
?
sn-2-acyl-phosphatidylcholine + 1,2-diacylglycerol
triacylglycerol + glycerophosphocholine
-
-
-
?
sn-2-acyl-phosphatidylcholine + 1,2-diacylglycerol
triacylglycerol + glycerophosphocholine
-
-
-
?
sn-2-acyl-phosphatidylcholine + 1,2-diacylglycerol
triacylglycerol + glycerophosphocholine
-
-
-
?
sn-2-acyl-phosphatidylcholine + 1,2-diacylglycerol
triacylglycerol + glycerophosphocholine
-
-
-
?
vernoloyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
vernoloyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
vernoloyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
vernoloyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
vernoloyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
vernoloyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
vernoloyl-phosphatidylcholine + 1,2-diacylglycerol
lyso-phosphatidylcholine + triacylglycerol
-
-
-
?
additional information
?
-
-
PDAT shows broad substrate specificity, overview
-
-
-
additional information
?
-
-
in the presence of alpha-linolenic acid, isoform PDAT1 produces triacylglycerol with a specific fatty acid composition. PDAT1 has the ability to synthesize trilinolenin, which is the major molecular species of triacylglycerol in flax oil
-
-
-
additional information
?
-
in the presence of alpha-linolenic acid, isoform PDAT1 produces triacylglycerol with a specific fatty acid composition. PDAT1 has the ability to synthesize trilinolenin, which is the major molecular species of triacylglycerol in flax oil
-
-
-
additional information
?
-
in the presence of alpha-linolenic acid, isoform PDAT1 produces triacylglycerol with a specific fatty acid composition. PDAT1 has the ability to synthesize trilinolenin, which is the major molecular species of triacylglycerol in flax oil
-
-
-
additional information
?
-
-
in the presence of alpha-linolenic acid, isoform PDAT2 produces triacylglycerol with a specific fatty acid composition. PDAT2 has the ability to synthesize trilinolenin, which is the major molecular species of triacylglycerol in flax oil
-
-
-
additional information
?
-
in the presence of alpha-linolenic acid, isoform PDAT2 produces triacylglycerol with a specific fatty acid composition. PDAT2 has the ability to synthesize trilinolenin, which is the major molecular species of triacylglycerol in flax oil
-
-
-
additional information
?
-
in the presence of alpha-linolenic acid, isoform PDAT2 produces triacylglycerol with a specific fatty acid composition. PDAT2 has the ability to synthesize trilinolenin, which is the major molecular species of triacylglycerol in flax oil
-
-
-
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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
phospholipid + 1,2-diacylglycerol
lysophospholipid + triacylglycerol
Q9FNA9
-
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
-
PDAT uses membrane lipids (e.g., phospholipids and glycolipids) as the substrates for the acyl transfer reaction or hydrolysis in vivo
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
-
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
the enzyme plays a major role in removing ricinoleic acid and vernolic acid from phospholipids in seeds
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
the enzyme plays a major role in removing ricinoleic acid and vernolic acid from phospholipids in seeds
-
?
phospholipid + 1,2-diacylglycerol
glycerolphosphocholine + triacylglycerol
-
-
-
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00138
-
sn-1,2-distearoylphosphatidylethanolamine as substrate using the membrane bound enzyme
0.001399
-
sn-1,2-dipalmitoylphosphatidylethanolamine as substrate using the membrane bound enzyme
0.002453
-
sn-1,2-dilinolenoylphosphatidylethanolamine as substrate using the membrane bound enzyme
0.002468
-
sn-1,2-dioleoylphosphatidylethanolamine as substrate using the membrane bound enzyme
0.002597
-
sn-1,2-dilinoleoylphosphatidylethanolamine as substrate using the membrane bound enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild type and mutants lacking wax ester synthase/acyl-coenzyme A: DAG acyltransferase DGAT activity
-
-
brenda
wild type and mutants lacking the acyl-CoA-independent acyltransferase activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
brenda
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
soluble form is produced for comparison with the native membrane bound enzyme
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
artificial microRNA silencing of PDAT alters the membrane lipid composition, reducing the maximum specific growth rate
physiological function
physiological function
-
upon expression of heterologous oleate 12-hydroxylase in Arabidopsis thaliana mutants deficient in phospholipid:diacylglycerol acyltransferases 1 or 2 accumulate hydroxy fatty acids and show no difference with wild-type plants. Mutants are also able to accumulate hydroxy fatty acids in seed neutral lipids. Individually, phospholipid:diacylglycerol acyltransferases 1 or 2 do not play a major role in the incorporation of hydroxy fatty acids into triacylglycerols
physiological function
-
phospholipid:diacylglycerol acyltransferase in the green microalga Chlamydomonas reinhardtii catalyzes triacylglycerol synthesis via two pathways: transacylation of diacylglycerol with acyl groups from phospholipids and galactolipids and diacylglycerol:diacylglycerol transacylation. PDAT-mediated membrane lipid turnover and triacylglycerol synthesis is essential for vigorous growth under favorable culture conditions and for membrane lipid degradation with concomitant production of triacylglycerol for survival under stress. PDAT also possesses acyl hydrolase activities using triacylglycerols, phospholipids, galactolipids, and cholesteryl esters as substrates
physiological function
expression of isoform DGTT1 complements the defect in the yeast DELTAdga1DELTAlro1 mutant that lacks the activity of triacylglycerol synthesis and leads to presence of oleic acid and lipid droplet formation; expression of isoform DGTT2 complements the defect in the yeast DELTAdga1DELTAlro1 mutant that lacks the activity of triacylglycerol synthesis. Complementation by DGTT2 increased triacylglycerol content by 9fold; expression of isoform DGTT3 complements the defect in the yeast DELTAdga1DELTAlro1 mutant that lacks the activity of triacylglycerol synthesis
physiological function
expression of isoform PDAT1 restores triacylglycerol synthesis in Saccharomyces cerevisiae H1246 when culturing yeast in the presence of alpha-linolenic acid; expression of isoform PDAT1 restores triacylglycerol synthesis in Saccharomyces cerevisiae H1246 when culturing yeast in the presence of alpha-linolenic acid
physiological function
-
overexpression of isoform PDAT1 increases leaf triacylglycerol accumulation, leading to oil droplet overexpansion through fusion. Ectopic expression of oleosin promotes the clustering of small oil droplets. Coexpression of PDAT1 with oleosin boosts leaf triacylglycerol content by up to 6.4% of the dry weight without affecting membrane lipid composition and plant growth. PDAT1 overexpression stimulates fatty acid synthesis and increases fatty acid flux toward the prokaryotic glycerolipid pathway. In the trigalactosyldiacylglycerol1-1 mutant, defective in eukaryotic thylakoid lipid synthesis, the combined overexpression of PDAT1 with oleosin increases leaf triacylglycerol content to 8.6% of the dry weight and total leaf lipid by fourfold. In the plastidic glycerol-3-phosphate acyltransferase1 mutant, defective in the prokaryotic glycerolipid pathway, PDAT1 overexpression enhances triacylglycerol content at the expense of thylakoid membrane lipids, leading to defects in chloroplast division and thylakoid biogenesis
Show AA Sequence and Transmembrane Helices (157 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
95000
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
104600
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
120000
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
enzyme contains 4 potential N-glycosylation sites at residues N161, N381, N434, and N647
glycoprotein
-
extensive deglycosylation severely decreases the activity
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of transgenic plants overexpressing the endogenous gene in leaves and roots, the transgenic plants show elevated enzyme activity
additional information
-
lipid analysis of enzyme knockout mutant by T-DNA insertion in locus At5g13640. Fatty acid content and composition in seeds does not show significant changes in the mutant. PDAT activity encoded by At5g13640 is not a major determinant of triacylglycerol synthesis in Arabidopsis seeds
additional information
construction of pdat, diacylglycerol O-acyltransferases (EC 2.3.1.20) dgat1 and dgat2 single mutants, of dgat1/dgat2 double mutant, and of a dgat1/dgat2/pdat triple mutant, which show 70%, 57%, 36%, 18% and 13%, respectively, of wild-type total lipid% per dry cell weight, phenotypes, overview
additional information
-
construction of pdat, diacylglycerol O-acyltransferases (EC 2.3.1.20) dgat1 and dgat2 single mutants, of dgat1/dgat2 double mutant, and of a dgat1/dgat2/pdat triple mutant, which show 70%, 57%, 36%, 18% and 13%, respectively, of wild-type total lipid% per dry cell weight, phenotypes, overview
-
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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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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, functional overexpression in Arabidopsis thaliana roots and leaves
-
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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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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
Arabidopsis thaliana, Crepis palaestina, Euphorbia lagascae, Ricinus communis
brenda
Dahlqvist, A.; Stahl, U.; Lenman, M.; Banas, A.; Lee, M.; Sandager, L.; Ronne, H.; Stymne, S.
Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants
Proc. Natl. Acad. Sci. USA
97
6487-6492
2000
Crepis palaestina, Helianthus annuus, Ricinus communis, Saccharomyces cerevisiae
brenda
Stahl, U.; Carlsson, A.S.; Lenman, M.; Dahlqvist, A.; Huang, B.; Banas, W.; Banas, A.; Stymne, S.
Cloning and functional characterization of a phospholipid:diacylglycerol acyltransferase from Arabidopsis
Plant Physiol.
135
1324-1335
2004
Arabidopsis thaliana (Q9FNA9)
brenda
Mhaske, V.; Beldjilali, K.; Ohlrogge, J.; Pollard, M.
Isolation and characterization of an Arabidopsis thaliana knockout line for phospholipid: diacylglycerol transacylase gene (At5g13640)
Plant Physiol. Biochem.
43
413-417
2005
Arabidopsis thaliana
brenda
Arabolaza, A.; Rodriguez, E.; Altabe, S.; Alvarez, H.; Gramajo, H.
Multiple pathways for triacylglycerol biosynthesis in Streptomyces coelicolor
Appl. Environ. Microbiol.
74
2573-2582
2008
Streptomyces coelicolor
brenda
Ghosal, A.; Banas, A.; Stahl, U.; Dahlqvist, A.; Lindqvist, Y.; Stymne, S.
Saccharomyces cerevisiae phospholipid:diacylglycerol acyl transferase (PDAT) devoid of its membrane anchor region is a soluble and active enzyme retaining its substrate specificities
Biochim. Biophys. Acta
1771
1457-1463
2007
Saccharomyces cerevisiae
brenda
Czabany, T.; Wagner, A.; Zweytick, D.; Lohner, K.; Leitner, E.; Ingolic, E.; Daum, G.
Structural and biochemical properties of lipid particles from the yeast Saccharomyces cerevisiae
J. Biol. Chem.
283
17065-17074
2008
Saccharomyces cerevisiae
brenda
Hernandez, M.L.; Guschina, I.A.; Martinez-Rivas, J.M.; Mancha, M.; Harwood, J.L.
The utilization and desaturation of oleate and linoleate during glycerolipid biosynthesis in olive (Olea europaea L.) callus cultures
J. Exp. Bot.
59
2425-2435
2008
Olea europaea
brenda
Dauk, M.; Lam, P.; Smith, M.
The role of diacylglycerol acyltransferase-1 and phospholipid: diacylglycerol acyltransferase-1 and -2 in the incorporation of hydroxy fatty acids into triacylglycerol in Arabidopsis thaliana expressing a castor bean oleate 12-hydroxylase gene
Botany
87
552-560
2009
Arabidopsis thaliana
-
brenda
Yoon, K.; Han, D.; Li, Y.; Sommerfeld, M.; Hu, Q.
Phospholipid:diacylglycerol acyltransferase is a multifunctional enzyme involved in membrane lipid turnover and degradation while synthesizing triacylglycerol in the unicellular green microalga Chlamydomonas reinhardtii
Plant Cell
24
3708-3724
2012
Chlamydomonas reinhardtii
brenda
van Erp, H.; Bates, P.D.; Burgal, J.; Shockey, J.; Browse, J.
Castor phospholipid:diacylglycerol acyltransferase facilitates efficient metabolism of hydroxy fatty acids in transgenic Arabidopsis
Plant Physiol.
155
683-693
2011
Ricinus communis
brenda
Zhang, H.; Damude, H.G.; Yadav, N.S.
Three diacylglycerol acyltransferases contribute to oil biosynthesis and normal growth in Yarrowia lipolytica
Yeast
29
25-38
2012
Yarrowia lipolytica (Q6C5M4), Yarrowia lipolytica, Yarrowia lipolytica ATCC 20362 (Q6C5M4)
brenda
Hung, C.H.; Ho, M.Y.; Kanehara, K.; Nakamura, Y.
Functional study of diacylglycerol acyltransferase type 2 family in Chlamydomonas reinhardtii
FEBS Lett.
587
2364-2370
2013
Chlamydomonas reinhardtii (A8INZ7), Chlamydomonas reinhardtii (A8J110), Chlamydomonas reinhardtii, Chlamydomonas reinhardtii (R9YW17)
brenda
Pan, X.; Siloto, R.M.; Wickramarathna, A.D.; Mietkiewska, E.; Weselake, R.J.
Identification of a pair of phospholipid:diacylglycerol acyltransferases from developing flax (Linum usitatissimum L.) seed catalyzing the selective production of trilinolenin
J. Biol. Chem.
288
24173-24188
2013
Linum usitatissimum, Linum usitatissimum (V5LWK6), Linum usitatissimum (V5LY10)
brenda
Fan, J.; Yan, C.; Zhang, X.; Xu, C.
Dual role for phospholipid:diacylglycerol acyltransferase: enhancing fatty acid synthesis and diverting fatty acids from membrane lipids to triacylglycerol in Arabidopsis leaves
Plant Cell
25
3506-3518
2013
Arabidopsis thaliana (Q9FNA9)
brenda
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