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Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.3.1.158 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)

EC Number Cloned (Comment) Organism
2.3.1.158 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
2.3.1.158 infiltrated into the lower epidermal cells of tobacco leaves via Agrobacterium tumefaciens GV3101 Lobosphaera incisa

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.158 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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

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

Expression

EC Number Organism Comment Expression
2.3.1.158 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

EC Number General Information Comment Organism
2.3.1.158 metabolism the enzyme contributes to the conversion of membrane lipids into triacylglycerol in Myrmecia incisa during the nitrogen starvation stress Lobosphaera incisa
2.3.1.158 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
2.3.1.158 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