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Literature summary extracted from

  • Zhang, Q.Y.; Niu, L.X.; Yu, R.; Zhang, X.X.; Bai, Z.Z.; Duan, K.; Gao, Q.H.; Zhang, Y.L.
    Cloning, characterization, and expression analysis of a gene encoding a putative lysophosphatidic acid acyltransferase from seeds of Paeonia rockii (2017), Appl. Biochem. Biotechnol., 182, 721-741 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.51 gene PrLPAAT1, DNA and amino acid sequence determination and analysis, domain structure, phylogenetic analysis, quantitative real-time RT-PCR enzyme expression analysis, recombinant overexpression using a seed-specific promoter in Arabidopsis thaliana plants, recombinant expression of GFP-tagged enzyme in the lower epidermis of Nicotiana tabacum leaves by Agrobacterium-mediated transformation method Paeonia rockii

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.51 additional information recombinant overexpression of gene PrLPAAT1 in Arabidopsis thaliana transgenic plant seeds increases total fatty acid (FA) content and the main fatty acid accumulation. Most of the FAs have higher levels of production in the transgenic T1 seeds compared to wild-type seeds, and the predominant FAs in the transgenic seeds are C18:1, C18:2, C18:3, C20:1, and C16:0 Paeonia rockii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.51 additional information subcelluar localization study in transgenic Nicotiana tabacum leaves Paeonia rockii
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2.3.1.51 plasma membrane the enzyme contains two transmembrane domains Paeonia rockii 5886
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate Paeonia rockii enzyme LPAAT catalyzes lysophosphatidic acid to yield phosphatidic acid by acylation of the sn-2 position of glycerol 3-phosphate. LPAAT is able to discriminate acyl groups with different chain lengths and possesses a selectivity and specificity for unsaturated C18 acyl groups in traditional oil seed crops CoA + 1,2-diacyl-sn-glycerol 3-phosphate
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.51 Paeonia rockii KX256278
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.51 flower
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 Paeonia rockii
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2.3.1.51 additional information PrLPAAT1 is ubiquitously expressed in diverse tissues, the expression is higher in the flower and developing seed, isozyme expression profile and fatty acid contents in different organs as well as in seeds at different developmental stages, overview Paeonia rockii
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2.3.1.51 seed analysis of enzyme expression during seed development, overview. PrLPAAT1 expression has a biphasic pattern. PrLPAAT1 exhibits relatively high transcript abundance during S1-S6 and drops thereafter (S6-S9). The expression of the PrLPAAT1 gene is increased at S1-S6, which coincides with the highest rate of fatty acid accumulation in tree peony seeds Paeonia rockii
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
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 Paeonia rockii CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate enzyme LPAAT catalyzes lysophosphatidic acid to yield phosphatidic acid by acylation of the sn-2 position of glycerol 3-phosphate. LPAAT is able to discriminate acyl groups with different chain lengths and possesses a selectivity and specificity for unsaturated C18 acyl groups in traditional oil seed crops Paeonia rockii CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.51 ? x * 38800, about, sequence calculation Paeonia rockii
2.3.1.51 More conserved domain analysis, and PrLPAAT1 tertiary structural modelling. The enzyme contains conserved 1-acyl-sn-glycerol-3-phosphate acyltransferase-related (PLN02901) and LPLAT_AGPAT-like (cd07989) domain Paeonia rockii

Synonyms

EC Number Synonyms Comment Organism
2.3.1.51 acyl-CoA:1-acylglycerol-sn-3-phosphate acyltransferase
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 Paeonia rockii
2.3.1.51 AGPAT
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 Paeonia rockii
2.3.1.51 LPAAT
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 Paeonia rockii
2.3.1.51 lysophosphatidic acid acyltransferase
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 Paeonia rockii
2.3.1.51 PrLPAAT1
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 Paeonia rockii

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.3.1.51 Paeonia rockii sequence calculation
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 9.68

General Information

EC Number General Information Comment Organism
2.3.1.51 evolution PrLPAAT1 may be a member of AGPAT family, and may have acyltransferase activity, comparisons of sequences, genetic structures, and conserved structure motifs, overview. Phylogenetic analysis Paeonia rockii
2.3.1.51 metabolism through the conventional Kennedy pathway in the endoplasmic reticulum, triacylglycerol (TAG) is synthesized de novo in three acylation reactions at the sn-1-, sn-2-, and sn-3-positions of the glycerol-3-phosphate backbone with acyl chains from acyl-CoAs, and these three reactions respectively are catalyzed by glycerol-3-phosphate acyltransferase (GPAT, EC 2.3.1.15), LPAAT, and diacylglycerol acyltransferase (DGAT, EC 2.3.1.20) Paeonia rockii
2.3.1.51 additional information PrLPAAT1 structure prediction and modelling, overview Paeonia rockii
2.3.1.51 physiological function PrLPAAT1 is an important component in the fatty acid accumulation process, especially during the early stages of seed development. LPAAT is able to discriminate acyl groups with different chain lengths and possesses a selectivity and specificity for unsaturated C18 acyl groups in traditional oil seed crops Paeonia rockii