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Literature summary for 2.3.1.51 extracted from

  • Zhang, Q.; Yu, R.; Sun, D.; Bai, Z.; Li, H.; Xue, L.; Zhang, Y.; Niu, L.
    PrLPAAT4, a putative lysophosphatidic acid acyltransferase from Paeonia rockii, plays an important role in seed fatty acid biosynthesis (2017), Molecules, 22, 1694-1707 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene LPAAT4, isolated from seed of unsaturated fatty acid (UFA)-rich Paeonia rockii, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant overexpression of the enzyme in Arabidopsis thaliana resulting in a significant increase in the content of oleic acid (OA) and total fatty acids (FAs) in seeds. AtDGAT1, AtGPAT9, and Atoleosin, involved in TAG assembly, are upregulated in PrLPAAT4-overexpressing lines. Recombinnat expression of GFP-tagged enzyme in tobacco lower epidermal cell plama membranes Paeonia rockii

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane a transmembrane enzyme, it exhibits an overlap between the transmembrane and LPLAT_AGPAT-like domains Paeonia rockii 5886
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Organism

Organism UniProt Comment Textmining
Paeonia rockii KX256279
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Source Tissue

Source Tissue Comment Organism Textmining
additional information tissue-specific expression profile of PrLPAAT4 Paeonia rockii
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seed
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Paeonia rockii
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Subunits

Subunits Comment Organism
? x * 42900, about, sequence calculation Paeonia rockii

Synonyms

Synonyms Comment Organism
LPAAT4
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Paeonia rockii
lysophosphatidic acid acyltransferase
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Paeonia rockii
lysophosphatidyl acyltransferase 4
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Paeonia rockii

General Information

General Information Comment Organism
evolution the enzyme belongs to the acyl-CoA:1-acylglycerol-sn-3-phosphate acyltranferases (AGPAT) family, PrLPAAT4 possesses a 1-acyl-sn-glycerol-3-phosphate acyltransferase-related domain, it is subordinated to cluster III. Comparative analysis of gene structure and conserved domain in the LPAAT4 proteins Paeonia rockii
metabolism PrLPAAT4 plays an important role in seed fatty acid biosynthesis Paeonia rockii
additional information comparative structure deduction and analysis of PrLPAAT4 Paeonia rockii
physiological function lysophosphatidic acid acyltransferases (LPAATs) are essential for the acylation of lysophosphatidic acid (LPA) and the synthesis of phosphatidic acid (PA), a key intermediate in the synthesis of membrane phospholipids and storage lipids. PrLPAAT4, a putative lysophosphatidic acid acyltransferase from Paeonia rockii, plays an important role in seed fatty acid biosynthesis. LPAATs play a crucial role in catalyzing the second step of triacylglycerol (TAG) formation, determining TAGs acyl composition at the sn-2-position, and controlling the conversion of LPA to PA. PrLPAAT4 might function as a positive regulator in seed fatty acid biosynthesis Paeonia rockii