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Literature summary extracted from

  • Panigrahi, R.; Matsui, T.; Song, A.H.; Caldo, K.M.P.; Young, H.S.; Weselake, R.J.; Lemieux, M.J.
    Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus (2018), Sci. Rep., 8, 16665 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.3.1.20 biofuel production DGAT1 is a target for genetic manipulation to increase seed oil production in oleaginous plants. Triacylglycerol produced by the enzyme can be a petrochemical alternative Brassica napus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.20 gene DGAT1, recombinant expression of N-terminally His-tagged enzyme cytoplasmic and autoinhibitory domains, BnaDGAT11-113 and BnaDGAT11-80, in Escherichia coli strain BL21(DE3), method optimization and evaluation, overview. The tag is located at the disordered N-terminal region, which is distal to the folded C-terminal region and the primary ligand binding site. Hence tag-induced secondary structure elements, if any, might not influence the ligand binding properties Brassica napus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.20 purified recombinnat truncated enzyme forms, BnaDGAT11-113 and BnaDGAT11-80, X-ray diffraction structure determination and analysis. Synchrotron small-angle X-ray scattering (SAXS) experiments are performed to obtain detailed 3D structural information on this disordered region of DGAT1, multi-state modeling Brassica napus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.20 additional information construction of truncated enzyme mutants, BnaDGAT11-113 comprises the full-length cytoplasmic domain, and BnaDGAT11-80 comprises the autoinhibitory domain, the truncated proteins are non-globular and monomeric in vitro Brassica napus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.20 CoA an allosteric modulator of DGAT1, interaction with the cytoplasmic N-terminal region, overview Brassica napus
2.3.1.20 additional information the cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites, conformational heterogeneity in the N-terminal domain of DGAT1 Brassica napus
2.3.1.20 oleoyl-CoA an allosteric modulator of DGAT1, interaction with the cytoplasmic N-terminal region, overview Brassica napus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.20 endoplasmic reticulum membrane
-
 Brassica napus 5789
-
2.3.1.20 additional information DGAT1 (BnaDGAT1) is a polytopic membrane protein in the endoplasmic reticulum (ER) with its N-terminal domain (residues 1-113) localized to the cytoplasm. Structure model of isozyme DGAT1-a transmembrane and cytosolic domains, overview Brassica napus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.20 8600
-
 recombinant His-tagged cytosolic domain BnaDGAT11-80, gel filtration Brassica napus
2.3.1.20 13900
-
 recombinant His-tagged cytosolic domain BnaDGAT11-113, gel filtration Brassica napus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Brassica napus
-
 CoA + 1,2,3-triacylglycerol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.20 Brassica napus K9LL63
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.20 recombinant His-tagged enzyme cytoplasmic and autoinhibitory domains BnaDGAT11-113 and BnaDGAT11-80 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography. TEV protease tag cleavage as well as enzyme protein concentration after affinity chromatography lead to protein aggregation and are omitted Brassica napus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Brassica napus CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 additional information interaction of CoA and oleoyl-CoA with the cytoplasmic N-terminal region (BnaDGAT11-113) of isoform BnaC.DGAT1.a. Truncated forms BnaDGAT11-113 and BnaDGAT11-80 interact with oleoyl-CoA or CoA with micromolar affinity, docking study and kinetics. The N-terminal domain of BnaDGAT1 has a higher affinity for thioester than free CoA. Interestingly, BnaDGAT11-80 also interacts with both ligands but with lower affinity. Ligand binding results in gain of secondary structure in mutants BnaDGAT11-113 and BnaDGAT11-80 Brassica napus ?
-
-
2.3.1.20 oleoyl-CoA + 1,2-diacyl-sn-glycerol
-
 Brassica napus CoA + 1,2-diacyl-3-oleoyl-glycerol
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.20 ? 1 * 21000, about, recombinant His-tagged cytosolic domain BnaDGAT11-113, sequence calculation, 1 * 10500, about, recombinant His-tagged autoinhibitory domain BnaDGAT11-80, sequence calculation Brassica napus

Synonyms

EC Number Synonyms Comment Organism
2.3.1.20 BnaC.DGAT1.a
-
 Brassica napus
2.3.1.20 DGAT1
-
 Brassica napus
2.3.1.20 diacylglycerol acyltransferase 1
-
 Brassica napus

General Information

EC Number General Information Comment Organism
2.3.1.20 additional information determination of conformational heterogeneity in the N-terminal domain of DGAT1, disorder propensity for the full-length BnaDGAT11-501 sequence, overview. A small gain of secondary structure is induced by ligand binding. The cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites Brassica napus
2.3.1.20 physiological function intrinsic disorder in plant proteins has been reported to be essential for the stress response. An intrinsically disordered region (IDR) spanning the N-terminal cytosolic domain of the intramembrane enzyme diacylglycerol acyltransferase1 (DGAT1) from canola-type Brassica napus, has been identified. The IDR spans amino acid residues 1-80, while residues 81-113 have a folded structure. DGAT1 (EC 2.3.1.20) catalyzes the acyl-coenzyme A (CoA)-dependent acylation of sn-1, 2-diacylglycerol (DAG) to produce triacylglycerol (TAG) and CoA. TAG serves as an energy source for germination in plants, a component of edible oil. This enzyme has a substantial effect on carbon flux into seed oil Brassica napus