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Literature summary for 2.3.1.15 extracted from

  • Huang, L.; Yu, L.; Li, Z.; Li, Y.; Yoon, K.; Hu, Q.; Yuan, L.; Han, D.
    Microalgal plastidial lysophosphatidic acid acyltransferase interacts with upstream glycerol-3-phosphate acyltransferase and defines its substrate selectivity via the two transmembrane domains (2020), Algal Res., 45, 101758 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
partial-length cDNA of CrGPATcl with the omitted coding sequence for the predicted chloroplast transit peptide (i.e. residues 1-20) is amplified from a cDNA library of Chlamydomonas reinhardtii, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain M15 Chlamydomonas reinhardtii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information kinetics of the CrLPAAT1-CrGPATcl interaction, overview Chlamydomonas reinhardtii

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
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Chlamydomonas reinhardtii 9507
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + sn-glycerol 3-phosphate Chlamydomonas reinhardtii
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CoA + 1-acyl-sn-glycerol 3-phosphate
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?
additional information Chlamydomonas reinhardtii plastidial lysophosphatidic acid acyltransferase (CrLPAAT1, EC 2.3.1.51) is found to be interacting with the water-soluble plastidial glycerol-3-phosphate acyltransferase (CrGAPTcl) via its two transmembrane domains in vitro. The interaction between CrLPAAT1 and CrGPATcl can be negatively regulated by both the acyl-CoAs and lysophosphatidic acid in a dosage-dependent manner. Recombinant CrLPAAT1(wild-type) and CrLPAAT1(mut) and the control Trx-S-His6-tag protein in concentration gradients are incubated with the immobilized CrGPATcl, respectively. These recombinant proteins except CrGPATcl have the S tag and can be detected by anti-S tag antibody. Simultaneously, anti-CrGPATcl antibody is used for interaction detection in Western blotting. Kinetics of the CrLPAAT1-CrGPATcl interaction, overview. The stability of CrLPAAT1-CrGPATcl complex is inversely proportional to the concentrations of acyl donors used in the assays, and it is most sensitive to the high-concentration of C18:1 (n9)-CoA among various acyl donors ?
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Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii A0A2K3E3Z9
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography and ultrafiltration Chlamydomonas reinhardtii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + sn-glycerol 3-phosphate
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Chlamydomonas reinhardtii CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
additional information plastidial lysophosphatidic acid acyltransferase (CrLPAAT1, EC 2.3.1.51) is found to be interacting with the water-soluble plastidial glycerol-3-phosphate acyltransferase (CrGAPTcl) via its two transmembrane domains in vitro. The interaction between CrLPAAT1 and CrGPATcl can be negatively regulated by both the acyl-CoAs and lysophosphatidic acid in a dosage-dependent manner. Recombinant CrLPAAT1(wild-type) and CrLPAAT1(mut) and the control Trx-S-His6-tag protein in concentration gradients are incubated with the immobilized CrGPATcl, respectively. These recombinant proteins except CrGPATcl have the S tag and can be detected by anti-S tag antibody. Simultaneously, anti-CrGPATcl antibody is used for interaction detection in Western blotting. Kinetics of the CrLPAAT1-CrGPATcl interaction, overview. The stability of CrLPAAT1-CrGPATcl complex is inversely proportional to the concentrations of acyl donors used in the assays, and it is most sensitive to the high-concentration of C18:1 (n9)-CoA among various acyl donors Chlamydomonas reinhardtii ?
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Synonyms

Synonyms Comment Organism
CrGAPTcl
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Chlamydomonas reinhardtii
glycerol-3-phosphate acyltransferase
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Chlamydomonas reinhardtii
water-soluble plastidial glycerol-3-phosphate acyltransferase
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Chlamydomonas reinhardtii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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assay at Chlamydomonas reinhardtii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
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assay at Chlamydomonas reinhardtii

General Information

General Information Comment Organism
metabolism in microalgae, de novo biosynthesis of triacylglycerol (TAG) via the Kennedy pathway involves successive acylation of glycerol-3-phosphate (G-3-P) by glycerol-3-phosphate acyltransferase (GPAT, EC 2.3.1.15), lysophosphatidic acid acyltransferase (LPAAT, EC 2.3.1.51) and diacylglycerol acyltransferase (DGAT, EC 2.3.1.20). Microalgal plastidial lysophosphatidic acid acyltransferase (LPAAT1, EC 2.3.1.51) interacts with upstream glycerol-3-phosphate acyltransferase and defines its substrate selectivity via the two transmembrane domains. The interaction between LPAAT1 and GPATcl can be negatively regulated by both the acyl-CoAs and lysophosphatidic acid, regulation pattern, overview Chlamydomonas reinhardtii