Literature summary for 2.3.1.158 extracted from

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 (2016), Sci. Rep., 6, 26610 .

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	Lobosphaera incisa

Cloned(Commentary)

Cloned (Comment)	Organism
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	Lobosphaera incisa
infiltrated into the lower epidermal cells of tobacco leaves via Agrobacterium tumefaciens GV3101	Lobosphaera incisa

Cloned (Comment)

Organism

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

Lobosphaera incisa

infiltrated into the lower epidermal cells of tobacco leaves via Agrobacterium tumefaciens GV3101

Lobosphaera incisa

Protein Variants

Protein Variants	Comment	Organism
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	Lobosphaera incisa

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast envelope	-	Lobosphaera incisa	9941	-
chloroplast outer membrane	-	Lobosphaera incisa	9707	-
plasma membrane	-	Lobosphaera incisa	5886	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
phospholipid + 1,2-diacyl-sn-glycerol	Lobosphaera incisa	-	lysophospholipid + triacylglycerol	-	?
phospholipid + 1,2-diacyl-sn-glycerol	Lobosphaera incisa Reisigl H4301	-	lysophospholipid + triacylglycerol	-	?

Organism

Organism	UniProt	Comment	Textmining
Lobosphaera incisa	A0A173GQ96	-	-
Lobosphaera incisa	A0A173GQ96	i.e. Lobosphaera incisa	-
Lobosphaera incisa Reisigl H4301	A0A173GQ96	i.e. Lobosphaera incisa	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
phospholipid + 1,2-diacyl-sn-glycerol	-	Lobosphaera incisa	lysophospholipid + triacylglycerol	-	?
phospholipid + 1,2-diacyl-sn-glycerol	-	Lobosphaera incisa Reisigl H4301	lysophospholipid + triacylglycerol	-	?

Synonyms

Synonyms	Comment	Organism
MiPDAT	-	Lobosphaera incisa
PDAT	-	Lobosphaera incisa
phospholipid: diacylglycerol acyltransferase	-	Lobosphaera incisa

Expression

Organism	Comment	Expression
Lobosphaera incisa	variations of the phospholipid (PL) levels and the transcriptional levels of MiPDAT in Myrmecia incisa during nitrogen starvation stress, overview	up

General Information

General Information	Comment	Organism
metabolism	the enzyme contributes to the conversion of membrane lipids into triacylglycerol in Myrmecia incisa during the nitrogen starvation stress	Lobosphaera incisa
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	Lobosphaera incisa
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	Lobosphaera incisa