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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
- diacylglycerols
-
acyl-coa:diacylglycerol
-
biodiesel
-
acyltransferase1
-
presenile
-
acyl-coa-dependent
- biotechnology
- camelina
- accase
-
oleosins
- lpcat
- energy production
- synthesis
- industry
- molecular biology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase, At3g44830, At5g13640, AtPDAT1, AtPDAT2, CHLREDRAFT_184281, CHLREDRAFT_188937, CsPDAT1-A, CsPDAT1-B, CsPDAT1-C, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase
LRO1
MiPDAT
PDAT
PDAT1
PDAT2
phospholipid: diacylglycerol acyltransferase
phospholipid:diacylglycerol acyltransferase
YNR008w
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase
-
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase
-
-
PDAT
-
-
-
-
PDAT
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
-
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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
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-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-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
Lobosphaera incisa Reisigl H4301
-
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
-
-
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
the enzyme is capable of using broad acyl donors such as PA, PS, PG, monogalactosyldiacylglycerol, digalactosyldiacylglycerol, and acyl-CoA. The enzyme is more likely to use unsaturated acyl donors comparing 18:0/18:1 to 18:0/18:0 phospholipids. With regard to acyl acceptors, the enzyme prefers 1,2 to 1,3-diacylglycerol, while 12:0/12:0 1,3-diacylglycerol is identified as the optimal acyl acceptor, followed by 18:1/18:1 and 18:1/16:0 1,3-diacylglycerol
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
the enzyme is capable of using broad acyl donors such as PA, PS, PG, monogalactosyldiacylglycerol, digalactosyldiacylglycerol, and acyl-CoA. The enzyme is more likely to use unsaturated acyl donors comparing 18:0/18:1 to 18:0/18:0 phospholipids. With regard to acyl acceptors, the enzyme prefers 1,2 to 1,3-diacylglycerol, while 12:0/12:0 1,3-diacylglycerol is identified as the optimal acyl acceptor, followed by 18:1/18:1 and 18:1/16:0 1,3-diacylglycerol
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
XP_011088820, XP_020553631
-
-
-
?
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
-
-
?
additional information
?
-
Saccharoymces cerevisiae PDAT also displays low DAG:DAG transacylase activity
-
-
-
additional information
?
-
Saccharoymces cerevisiae PDAT also displays low DAG:DAG transacylase activity
-
-
-
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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
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-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-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
Lobosphaera incisa Reisigl H4301
-
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
-
-
-
-
?
phospholipid + 1,2-diacyl-sn-glycerol
lysophospholipid + triacylglycerol
XP_011088820, XP_020553631
-
-
-
?
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Long-term survival, place of death, and death certification in clinically diagnosed pre-senile dementia in northern England. Follow-up after 8-12 years.
Bacterial Infections
White light-triggered zwitterionic polymer nanoparticles based on an AIE-active photosensitizer for photodynamic antimicrobial therapy.
Corneal Perforation
Long-term outcomes of riboflavin photodynamic antimicrobial therapy as a treatment for infectious keratitis.
Dementia
Clinically diagnosed presenile dementia of the Alzheimer type in the Northern Health Region: ascertainment, prevalence, incidence and survival.
Dementia
Long-term survival, place of death, and death certification in clinically diagnosed pre-senile dementia in northern England. Follow-up after 8-12 years.
Dementia
Risk factors in clinically diagnosed presenile dementia of the Alzheimer type: a case-control study in northern England.
Hepatitis C
The Phospholipid:Diacylglycerol Acyltransferase Lro1 Is Responsible for Hepatitis C Virus Core-Induced Lipid Droplet Formation in a Yeast Model System.
Infections
A pH/H2O2 dual triggered nanoplatform for enhanced photodynamic antibacterial efficiency.
Infections
Rose bengal photodynamic antimicrobial therapy to inhibit Pseudomonas aeruginosa keratitis isolates.
Infections
Rose Bengal Photodynamic Antimicrobial Therapy: A Novel Treatment for Resistant Fusarium Keratitis.
Keratitis
Long-term outcomes of riboflavin photodynamic antimicrobial therapy as a treatment for infectious keratitis.
Keratitis
Rose Bengal Photodynamic Antimicrobial Therapy: A Novel Treatment for Resistant Fusarium Keratitis.
Prostatic Neoplasms
Is Primary Androgen Deprivation Therapy a Suitable Option for Asian Patients With Prostate Cancer Compared With Radical Prostatectomy?
Pseudomonas Infections
Rose bengal photodynamic antimicrobial therapy to inhibit Pseudomonas aeruginosa keratitis isolates.
Starvation
Changes in the photosynthetic apparatus and lipid droplet formation in Chlamydomonas reinhardtii under iron deficiency.
Starvation
Phospholipid: diacylglycerol acyltransferase contributes to the conversion of membrane lipids into triacylglycerol in Myrmecia incisa during the nitrogen starvation stress.
Starvation
Three acyltransferases and a nitrogen responsive regulator are implicated in nitrogen starvation-induced triacylglycerol accumulation in Chlamydomonas.
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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
6.05
6.33
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculated from sequence, CsPDAT1-A
6.43
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculated from sequence, CsPDAT1-C
8.56
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculated from sequence, CsPDAT2-A
8.61
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculated from sequence, CsPDAT2-B
6.05
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculated from sequence, CsPDAT1-B
6.05
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculated from sequence, CsPDAT2-B
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
GenBank
brenda
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
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
CsPDAT1-C preferentially accumulates in flower and leaf tissues
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-A
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-B
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT2-A
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT2-B
brenda
AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
CsPDAT1-C preferentially accumulates in flower and leaf tissues
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-A
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-B
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT2-A
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT2-B
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
high expression of CsPDAT2-A is detected in stem and root tissues
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
high expression of CsPDAT2-B is detected in stem and root tissues
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-A
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-B
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-C
brenda
AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
CsPDAT1-A is mainly expressed in seeds
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
intermediate activity, CsPDAT1-C
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-B
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT2-A
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT2-B
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
high expression of CsPDAT2-A is detected in stem and root tissues
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
high expression of CsPDAT2-B is detected in stem and root tissues
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-A
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-B
brenda
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
low activity, CsPDAT1-C
brenda
additional information
isozyme AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds, whereas isozyme AtPDAT2 is highly expressed in seeds
brenda
additional information
isozyme AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds, whereas isozyme AtPDAT2 is highly expressed in seeds
brenda
additional information
XP_010419957.1
different members of Camelina sativa phospholipid diacylglycerol acyltransferase family contribute to triacylglycerol synthesis in different tissues
brenda
additional information
XP_010453452.1
different members of Camelina sativa phospholipid diacylglycerol acyltransferase family contribute to triacylglycerol synthesis in different tissues
brenda
additional information
XP_010492131.1
different members of Camelina sativa phospholipid diacylglycerol acyltransferase family contribute to triacylglycerol synthesis in different tissues
brenda
additional information
XP_010503132.1
different members of Camelina sativa phospholipid diacylglycerol acyltransferase family contribute to triacylglycerol synthesis in different tissues
brenda
additional information
XP_010514811.1
different members of Camelina sativa phospholipid diacylglycerol acyltransferase family contribute to triacylglycerol synthesis in different tissues
brenda
additional information
-
different members of Camelina sativa phospholipid diacylglycerol acyltransferase family contribute to triacylglycerol synthesis in different tissues
brenda
additional information
XP_011088820
tissue distribution analysis by quantitative real-time PCR. SiPDAT1 expression is highest at flowering stage and developing seeds
brenda
additional information
XP_020553631
tissue distribution analysis by quantitative real-time PCR. SiPDAT1 expression is highest at flowering stage and developing seeds
brenda
additional information
XP_011088820
tissue distribution analysis by quantitative real-time PCR. SiPDAT2 expression is highest in stem and developing seeds
brenda
additional information
XP_020553631
tissue distribution analysis by quantitative real-time PCR. SiPDAT2 expression is highest in stem and developing seeds
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
XP_011088820, XP_020553631
SiPDAT2 does not have any transmembrane domains
-
brenda
additional information
-
soluble form is produced for comparison with the native membrane bound enzyme
brenda
additional information
phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
-
brenda
additional information
phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
-
brenda
additional information
-
phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
-
brenda
additional information
-
phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
-
brenda
additional information
phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
-
brenda
additional information
-
phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
-
brenda
additional information
phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
-
brenda
additional information
phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
-
brenda
additional information
-
phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
evolution
phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
evolution
-
phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
evolution
-
phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
evolution
two PDAT orthologues, AtPDAT1 and AtPDAT2, with 57% amino acid sequence similarity, are identified in Arabidopsis thaliana. Phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1
malfunction
-
artificial microRNA silencing of PDAT alters the membrane lipid composition, reducing the maximum specific growth rate
malfunction
-
LRO1 single knockout has a markedly reduced level of the coreinduced LD formation
malfunction
seedlings deficient in the enzyme PDAT1 are unable to accumulate triacylglycerols after heat stress
malfunction
the removal of the putative N-terminal transmembrane domain (TMD) in Saccharomyces cerevisiae PDAT does not affect activity
malfunction
-
the removal of the putative N-terminal transmembrane domain (TMD) in Saccharomyces cerevisiae PDAT does not affect activity
-
metabolism
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
different members of Camelina sativa phospholipid diacylglycerol acyltransferase family are involved in different types of stress responses in camelina seedlings, providing evidence of their roles in oil biosynthesis and regulation in camelina vegetative tissue
metabolism
XP_011088820, XP_020553631
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis
metabolism
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1, 2-DAG to yield TAG. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG
metabolism
-
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG
metabolism
-
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG
metabolism
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG
metabolism
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG
metabolism
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG
metabolism
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. PDAT and DGAT2 are the major contributors to TAG biosynthesis and their relative contributions were dependent on the yeast growth stage
metabolism
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
the enzyme catalyses the final acylation step in triacylglycerol biosynthesis by transferring a fatty acyl moiety from a phospholipid to diacylglycerol
metabolism
the enzyme catalyzes the acyl-CoA-independent synthesis of triacylglycerol using membrane glycerolipids as acyl donors
metabolism
the enzyme contributes to the conversion of membrane lipids into triacylglycerol in Myrmecia incisa during the nitrogen starvation stress
metabolism
the enzyme is a major determinant of triacylglycerol biosynthesis at the exponential growth stage. Overexpression of AtPDAT1 results in no effects on the fatty-acid and lipid composition, despite the fact that increased PDAT activity is observed in microsomes prepared from AtPDAT1 Arabidopsis overexpressor lines. PDAT1 is a dominant determinant in Arabidopsis seed triacylglycerol biosynthesis in the absence of DGAT1 activity
metabolism
-
the enzyme is responsible for Hepatitis C Virus core-induced lipid droplet formation in yeast
metabolism
the enzyme is responsible for the last step of triacylglycerol synthesis in the acyl-CoA-independent pathway, catalyzing membrane lipid transformation
metabolism
the enzyme plays an important role in triacylglycerol synthesis
metabolism
triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of sn-1, 2-DAG to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1, 2-DAG to yield TAG. The gradually increased transcription levels of MiPDAT in Myrmecia incisa during the cultivation under nitrogen starvation conditions is proposed to be responsible for the decrease and increase of the phosphatidylcholine and TAG levels, respectively
metabolism
-
the enzyme is responsible for the last step of triacylglycerol synthesis in the acyl-CoA-independent pathway, catalyzing membrane lipid transformation
-
metabolism
-
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. PDAT and DGAT2 are the major contributors to TAG biosynthesis and their relative contributions were dependent on the yeast growth stage
-
metabolism
-
the enzyme catalyzes the acyl-CoA-independent synthesis of triacylglycerol using membrane glycerolipids as acyl donors
-
metabolism
Lobosphaera incisa Reisigl H4301
-
the enzyme contributes to the conversion of membrane lipids into triacylglycerol in Myrmecia incisa during the nitrogen starvation stress
-
metabolism
Lobosphaera incisa Reisigl H4301
-
triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of sn-1, 2-DAG to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1, 2-DAG to yield TAG. The gradually increased transcription levels of MiPDAT in Myrmecia incisa during the cultivation under nitrogen starvation conditions is proposed to be responsible for the decrease and increase of the phosphatidylcholine and TAG levels, respectively
-
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
physiological function
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
physiological function
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
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
physiological function
MiPDAT links triacylglycerol (TAG) accumulation with phospholipid during the course of nitrogen starvation. This enzyme transfers an acyl group from the sn-2 position of phospholipids (PLs) to the sn-3 position of diacylglycerol (DAG), yielding sn-1-lysophospholipid and TAG, respectively. The temporal and spatial evidence for MiPDAT contributing to the conversion of membrane lipids into TAG Myrmecia incisa during nitrogen starvation stress is provided, MiPDAT can use membrane phosphatidylcholine to synthesize TAG in the microalgae grown under nitrogen starvation stress
physiological function
PDAT1-mediated triacylglycerol accumulation increases heat resistance
physiological function
XP_011088820, XP_020553631
phospholipid:diacylglycerol acyltransferase (PDAT) is an acyl-CoA-independent pathway enzyme using phosphatidylcholine (PC) as the acyl donor, in which the transfer of an acyl group from the sn-2 position of phosphatidylcholine to the sn-3 position of DAG yields triacylglycerol (TAG)
physiological function
-
triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine
physiological function
-
triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine
physiological function
triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine
physiological function
triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine
physiological function
triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine
physiological function
triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine
physiological function
-
triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine
-
physiological function
Lobosphaera incisa Reisigl H4301
-
MiPDAT links triacylglycerol (TAG) accumulation with phospholipid during the course of nitrogen starvation. This enzyme transfers an acyl group from the sn-2 position of phospholipids (PLs) to the sn-3 position of diacylglycerol (DAG), yielding sn-1-lysophospholipid and TAG, respectively. The temporal and spatial evidence for MiPDAT contributing to the conversion of membrane lipids into TAG Myrmecia incisa during nitrogen starvation stress is provided, MiPDAT can use membrane phosphatidylcholine to synthesize TAG in the microalgae grown under nitrogen starvation stress
-
additional information
comparison to human enzyme LCAT (EC 2.3.1.43)
additional information
-
comparison to human enzyme LCAT (EC 2.3.1.43)
-
Show AA Sequence and Transmembrane Helices (199 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
65953
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculation from sequence, CsPDAT1-B
73627
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculation from sequence, CsPDAT2-A
73721
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculation from sequence, CsPDAT2-B
74301
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculation from sequence, CsPDAT1-A
74321
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
calculation from sequence, CsPDAT1-C
95000
95000
-
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
glycoprotein
four glycosylation sites, the degree of glycosylation site N469 is the largest
glycoprotein
-
four glycosylation sites, the degree of glycosylation site N469 is the largest
-
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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
MiPDAT synthesizes TAG based on functional complementary experiments in the mutant yeast strain H1246 and the membrane lipid phosphatidylcholine (PC) is preferentially used as substrates as revealed by in vitro enzyme activity assay
additional information
-
MiPDAT synthesizes TAG based on functional complementary experiments in the mutant yeast strain H1246 and the membrane lipid phosphatidylcholine (PC) is preferentially used as substrates as revealed by in vitro enzyme activity assay
additional information
Lobosphaera incisa Reisigl H4301
-
MiPDAT synthesizes TAG based on functional complementary experiments in the mutant yeast strain H1246 and the membrane lipid phosphatidylcholine (PC) is preferentially used as substrates as revealed by in vitro enzyme activity assay
-
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
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
-
expression in tobacco leaves. The gene shows phospholipid diacylglycerol acyltransferase enzymatic activity and substantially increased triacylglycerol accumulation in the leaves
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
expression in tobacco leaves. The gene shows phospholipid diacylglycerol acyltransferase enzymatic activity and substantially increased triacylglycerol accumulation in the leaves. CsPDAT1-A shows a higher preference for alpha-linolenic acid (18:3 omega-3)
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
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
-
gene LRO1, DNA and amino acid sequence determination and analysis
gene MiPDAT, DNA and amino acid sequence determination and analysis, quantitative RT-PCR enzyme expression analysis, recombinant expression of GFP-tagged enzyme in Nicotiana benthamiana leaves via transfection method with Agrobacterium tumefaciens, subcloning in Escherichia coli strain DH5alpha, recombinant expression of PDAT in TAG-deficient Saccharomyces cerevisiae mutant strain H1246, complementation and lipid analysis, overview
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
gene SiPDAT, DNA and amino acid sequence determination and analysis, genetic structure, phylogenetic analysis, quantitative real-time PCR expression analysis, recombinant expression in TAG-deficient Saccharomyces cerevisiae mutant strain H1246 and complementation, higher oil content in SiPDAT gene-transformed mutants, lipid analysis, overview
XP_011088820, XP_020553631
gene SiPDAT, DNA and amino acid sequence determination and analysis, genetic structure, phylogenetic analysis, quantitative real-time PCR expression analysis, recombinant expression in TAG-deficient Saccharomyces cerevisiae mutant strain H1246 and complementation, higher oil content in SiPDAT gene-transformed mutants, SiPDAT1-expressing mutants have higher polyunsaturated (C18:1; C18:2) fatty acid content, lipid analysis, overview
XP_011088820, XP_020553631
infiltrated into the lower epidermal cells of tobacco leaves via Agrobacterium tumefaciens GV3101
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
-
overexpression in Arabidopsis thaliana increases alpha-linolenic acis content in seed oil
-
overexpression in Arabidopsis thaliana increases hydroxy fatty acid in seed oil
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
cold stress induces upregulation of CsPDAT1-A expression by 3.5fold compared to the control
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
cold stress induces upregulation of CsPDAT1-C expression by 2.5fold compared to the control
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
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
-
drought treatment results in a reduction of CsPDAT2-B expression
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
drought treatment results in an enhancement of CsPDAT2-A mRNAs by twofold
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
osmotic stress upregulates the expression of CsPDAT1-C by 3.3fold
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
salt stress leads to an increase in CsPDAT2-B transcript by 5.1fold
XP_010419957.1, XP_010453452.1, XP_010492131.1, XP_010503132.1, XP_010514811.1
the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
the R2R3-type MYB96 transcription factor was shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
variations of the phospholipid (PL) levels and the transcriptional levels of MiPDAT in Myrmecia incisa during nitrogen starvation stress, overview
the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
-
the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
-
the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
the R2R3-type MYB96 transcription factor was shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
the R2R3-type MYB96 transcription factor was shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
-
-
variations of the phospholipid (PL) levels and the transcriptional levels of MiPDAT in Myrmecia incisa during nitrogen starvation stress, overview
variations of the phospholipid (PL) levels and the transcriptional levels of MiPDAT in Myrmecia incisa during nitrogen starvation stress, overview
Lobosphaera incisa Reisigl H4301
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
energy production
-
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
-
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
-
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
-
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
biotechnology
-
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
-
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
Lobosphaera incisa Reisigl H4301
-
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
-
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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, Ricinus communis, Crepis palaestina, Euphorbia lagascae
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
Saccharomyces cerevisiae, Ricinus communis, Crepis palaestina, Helianthus annuus
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 (R9YW17), Chlamydomonas reinhardtii
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 (V5LWK6), Linum usitatissimum (V5LY10), Linum usitatissimum
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
Feng, Y.; Zhang, Y.; Ding, W.; Wu, P.; Cao, X.; Xue, S.
Expanding of phospholipid diacylglycerol acyltransferase (PDAT) from Saccharomyces cerevisiae as multifunctional biocatalyst with broad acyl donor/acceptor selectivity
Appl. Biochem. Biotechnol.
188
824-835
2019
Saccharomyces cerevisiae (P40345), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P40345)
brenda
Yuan, L.; Mao, X.; Zhao, K.; Ji, X.; Ji, C.; Xue, J.; Li, R.
Characterisation of phospholipid diacylglycerol acyltransferases (PDATs) from Camelina sativa and their roles in stress responses
Biol. Open
6
1024-1034
2017
Camelina sativa (XP_010419957.1), Camelina sativa (XP_010453452.1), Camelina sativa (XP_010492131.1), Camelina sativa (XP_010503132.1), Camelina sativa (XP_010514811.1), Camelina sativa
brenda
Xu, Y.; Caldo, K.M.P.; Pal-Nath, D.; Ozga, J.; Lemieux, M.J.; Weselake, R.J.; Chen, G.
Properties and biotechnological applications of acyl-CoA diacylglycerol acyltransferase and phospholipid diacylglycerol acyltransferase from terrestrial plants and microalgae
Lipids
53
663-688
2018
Brassica napus, Ricinus communis, Ricinus communis (F2VR35), Crepis palaestina, Linum usitatissimum, Helianthus annuus (A0A251VCQ4), Saccharomyces cerevisiae (P40345), Arabidopsis thaliana (Q9FNA9), Arabidopsis thaliana (Q9FYC7), Saccharomyces cerevisiae ATCC 204508 (P40345)
brenda
Chellamuthu, M.; Kumaresan, K.; Subramanian, S.; Muthumanickam, H.
Functional analysis of sesame diacylglycerol acyltransferase and phospholipid diacylglycerol acyltransferase genes using in silico and in vitro approaches
Plant Mol. Biol. Rep.
37
146-156
2019
Sesamum indicum (XP_011088820), Sesamum indicum (XP_020553631)
-
brenda
Mueller, S.P.; Unger, M.; Guender, L.; Fekete, A.; Mueller, M.J.
Phospholipid diacylglycerol acyltransferase-mediated triacylglyerol synthesis augments basal thermotolerance
Plant Physiol.
175
486-497
2017
Arabidopsis thaliana (Q9FNA9)
brenda
Aulakh, K.; Durrett, T.P.
The plastid lipase PLIP1 is critical for seed viability in diacylglycerol acyltransferase1 mutant seed
Plant Physiol.
180
1962-1974
2019
Arabidopsis thaliana (Q9FNA9)
brenda
Iwasa, S.; Sato, N.; Wang, C.W.; Cheng, Y.H.; Irokawa, H.; Hwang, G.W.; Naganuma, A.; Kuge, S.
The Phospholipid diacylglycerol acyltransferase Lro1 is responsible for hepatitis C virus core-induced lipid droplet formation in a yeast model system
PLoS ONE
11
e0159324
2016
Saccharomyces cerevisiae
brenda
Liu, X.Y.; Ouyang, L.L.; Zhou, Z.G.
Phospholipid diacylglycerol acyltransferase contributes to the conversion of membrane lipids into triacylglycerol in Myrmecia incisa during the nitrogen starvation stress
Sci. Rep.
6
26610
2016
Lobosphaera incisa (A0A173GQ96), Lobosphaera incisa, Lobosphaera incisa Reisigl H4301 (A0A173GQ96)
brenda
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