Literature summary for 2.3.1.158 extracted from

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 (2018), Lipids, 53, 663-688 .

Search for more literature for 2.3.1.158

Application

Application	Comment	Organism
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	Brassica napus
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	Crepis palaestina
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	Arabidopsis thaliana
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	Helianthus annuus
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	Ricinus communis

Cloned(Commentary)

Cloned (Comment)	Organism
gene LRO1, DNA and amino acid sequence determination and analysis	Saccharomyces cerevisiae
overexpression in Arabidopsis thaliana increases alpha-linolenic acis content in seed oil	Linum usitatissimum
overexpression in Arabidopsis thaliana increases hydroxy fatty acid in seed oil	Ricinus communis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
microsome	-	Helianthus annuus	-	-
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	Crepis palaestina	-	-
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	Arabidopsis thaliana	-	-
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	Saccharomyces cerevisiae	-	-
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	Brassica napus	-	-
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	Helianthus annuus	-	-
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	Ricinus communis	-	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
acyl-CoA + 1,2-diacyl-sn-glycerol	Brassica napus	-	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	Crepis palaestina	-	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	Arabidopsis thaliana	-	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	Saccharomyces cerevisiae	-	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	Helianthus annuus	-	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	Ricinus communis	-	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	Saccharomyces cerevisiae ATCC 204508	-	CoA + 1,2,3-triacylglycerol	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9FNA9	-	-
Arabidopsis thaliana	Q9FYC7	-	-
Brassica napus	-	-	-
Crepis palaestina	-	-	-
Helianthus annuus	A0A251VCQ4	-	-
Linum usitatissimum	-	-	-
Ricinus communis	-	-	-
Ricinus communis	F2VR35	-	-
Saccharomyces cerevisiae	P40345	-	-
Saccharomyces cerevisiae ATCC 204508	P40345	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds	Arabidopsis thaliana	-
additional information	isozyme AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds, whereas isozyme AtPDAT2 is highly expressed in seeds	Arabidopsis thaliana	-
seed	-	Helianthus annuus	-
seed	high expression	Arabidopsis thaliana	-
seed	AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds	Arabidopsis thaliana	-
seed	highly expressed in seeds	Arabidopsis thaliana	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
acyl-CoA + 1,2-diacyl-sn-glycerol	-	Brassica napus	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	-	Crepis palaestina	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	-	Arabidopsis thaliana	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	-	Saccharomyces cerevisiae	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	-	Helianthus annuus	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	-	Ricinus communis	CoA + 1,2,3-triacylglycerol	-	?
acyl-CoA + 1,2-diacyl-sn-glycerol	-	Saccharomyces cerevisiae ATCC 204508	CoA + 1,2,3-triacylglycerol	-	?
additional information	Saccharoymces cerevisiae PDAT also displays low DAG:DAG transacylase activity	Saccharomyces cerevisiae	?	-	-
additional information	Saccharoymces cerevisiae PDAT also displays low DAG:DAG transacylase activity	Saccharomyces cerevisiae ATCC 204508	?	-	-

Synonyms

Synonyms	Comment	Organism
At3g44830	-	Arabidopsis thaliana
At5g13640	-	Arabidopsis thaliana
AtPDAT1	-	Arabidopsis thaliana
AtPDAT2	-	Arabidopsis thaliana
LRO1	-	Saccharomyces cerevisiae
PDAT	-	Brassica napus
PDAT	-	Ricinus communis
PDAT	-	Linum usitatissimum
PDAT	-	Crepis palaestina
PDAT	-	Arabidopsis thaliana
PDAT	-	Saccharomyces cerevisiae
PDAT	-	Helianthus annuus
PDAT1	-	Arabidopsis thaliana
PDAT2	-	Arabidopsis thaliana
phospholipid:diacylglycerol acyltransferase	-	Brassica napus
phospholipid:diacylglycerol acyltransferase	-	Crepis palaestina
phospholipid:diacylglycerol acyltransferase	-	Arabidopsis thaliana
phospholipid:diacylglycerol acyltransferase	-	Saccharomyces cerevisiae
phospholipid:diacylglycerol acyltransferase	-	Helianthus annuus
phospholipid:diacylglycerol acyltransferase	-	Ricinus communis
YNR008w	-	Saccharomyces cerevisiae

Expression

Organism	Comment	Expression
Brassica napus	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	up
Crepis palaestina	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	up
Arabidopsis thaliana	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	up
Helianthus annuus	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	up
Ricinus communis	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	up
Saccharomyces cerevisiae	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	up

General Information

General Information	Comment	Organism
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	Helianthus annuus
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	Ricinus communis
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	Brassica napus
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	Crepis palaestina
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	Arabidopsis thaliana
malfunction	the removal of the putative N-terminal transmembrane domain (TMD) in Saccharomyces cerevisiae PDAT does not affect activity	Saccharomyces cerevisiae
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	Arabidopsis thaliana
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	Brassica napus
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	Crepis palaestina
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	Arabidopsis thaliana
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	Helianthus annuus
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	Ricinus communis
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	Saccharomyces cerevisiae
metabolism	the enzyme catalyzes the acyl-CoA-independent synthesis of triacylglycerol using membrane glycerolipids as acyl donors	Saccharomyces cerevisiae
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	Arabidopsis thaliana
additional information	comparison to human enzyme LCAT (EC 2.3.1.43)	Saccharomyces cerevisiae
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	Brassica napus
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	Crepis palaestina
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	Arabidopsis thaliana
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	Saccharomyces cerevisiae
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	Helianthus annuus
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	Ricinus communis