Literature summary for 2.3.1.20 extracted from

Caldo, K.M.P.; Acedo, J.Z.; Panigrahi, R.; Vederas, J.C.; Weselake, R.J.; Lemieux, M.J.
Diacylglycerol acyltransferase 1 is regulated by Its N-terminal domain in response to allosteric effectors (2017), Plant Physiol., 175, 667-680 .

Search for more literature for 2.3.1.20

Cloned(Commentary)

Cloned (Comment)	Organism
isozyme BnaC.DGAT1.a, recombinant expression of wild-type and truncated mutant enzymes in Saccharomyces cerevisiae strain H1246, which is devoid of TAG biosynthesis	Brassica napus

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of several truncated enzyme versions of isozyme BnaC.DGAT1.a, BnaDGAT161-501 and BnaDGAT181-501 exhibit higher normalized specific activity compared with the full-length enzyme. Despite the lower production level of BnaDGAT161-501 and BnaDGAT181-501, these enzyme forms are able to generate TAG amounting to about 60% of the total triacylglycerol (TAG) produced by the full-length enzyme in situ. Mutant BnaDGAT1114-501,which is devoid of the entire N-terminal domain, is about 10fold less active than the full-length enzyme. The affinity of BnaDGAT1114-501 for acyl-CoA is much lower than that of the full-length BnaDGAT1 or BnaDGAT181-501. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site	Brassica napus

Inhibitors

Inhibitors	Comment	Organism	Structure
acyl-CoA	substrate inhibition is observed at higher concentrations of acyl-CoA	Brassica napus
CoA	noncompetitively inhibits isozyme BnaC.DGAT1.a. The N-terminal domain of isoform BnaA.DGAT1.b can interact with acyl-CoA at a possible allosteric site, and CoA can displace the thioester	Brassica napus
additional information	the highly disordered segment at the enzyme's N-terminus is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif	Brassica napus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	isozyme BnaC.DGAT1.a exhibits positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. Kinetics of wild-type and enzyme mutants, Michaelis-Menten kinetic model	Brassica napus
0.00055	-	oleoyl-CoA	pH 7.4, 30°C, recombinant truncated enzyme mutant BnaDGAT181-501	Brassica napus
0.00061	-	oleoyl-CoA	pH 7.4, 30°C, recombinant full-length wild-type enzyme	Brassica napus
0.00067	-	palmitoyl-CoA	pH 7.4, 30°C, recombinant truncated enzyme mutant BnaDGAT181-501	Brassica napus
0.00069	-	palmitoyl-CoA	pH 7.4, 30°C, recombinant full-length wild-type enzyme	Brassica napus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	DGAT1 has 8 to 10 transmembrane domains	Brassica napus	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Brassica napus

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Brassica napus	K9LL63	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acyl-CoA + 1,2-diacyl-sn-glycerol	-	Brassica napus	CoA + 1,2,3-triacylglycerol	-	?
additional information	the acyl-CoA binding site is located at N-terminal domain of DGAT1 along amino acid residues 81 to 113	Brassica napus	?	-	-
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol	-	Brassica napus	CoA + 1,2,3-trioleoylglycerol	-	?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol	-	Brassica napus	CoA + 1,2-dioleoyl-3-palmitoylglycerol	-	?

Subunits

Subunits	Comment	Organism
dimer	the BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction	Brassica napus
More	the full-length polypeptide is predominantly well folded (about 68% alpha-helices/beta-sheets), while the N-terminal domain only has about 29% alpha-helices/beta-sheets	Brassica napus

Synonyms

Synonyms	Comment	Organism
BnaC.DGAT1.a	-	Brassica napus
BnaDGAT1	-	Brassica napus
DGAT1	-	Brassica napus
diacylglycerol acyltransferase 1	-	Brassica napus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Brassica napus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Brassica napus

General Information

General Information	Comment	Organism
evolution	DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOATs). The DGAT1 family is highly conserved. DGAT1 possesses a very hydrophilic N-terminal region corresponding to about the first 100 residues, which is followed by eight to ten predicted transmembrane segments	Brassica napus
malfunction	BnaDGAT161-501 and BnaDGAT181-501 exhibit higher normalized specific activity compared with the full-length enzyme. Despite the lower production level of BnaDGAT161-501 and BnaDGAT181-501, these enzyme forms are able to generate TAG amounting to about 60% of the total triacylglycerol (TAG) produced by the full-length enzyme in situ. Mutant BnaDGAT1114-501, which is devoid of the entire N-terminal domain, is about 10fold less active than the full-length enzyme. The affinity of BnaDGAT1114-501 for acyl-CoA is much lower than that of the full-length BnaDGAT1 or BnaDGAT181-501. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site	Brassica napus
additional information	DGAT1 enzymes may be regulated through allosteric interactions. The self-association properties of DGAT1 enzymes are consistent with the fact that most allosteric enzymes exhibit quaternary structure, identification of CoA/acyl-CoA binding site in the hydrophilic N-terminal domain and specific interactions involved in CoA recognition, and analysis of structure and function of the hydrophilic N-terminal domain of Brassica napus DGAT1, overview. This domain is found to have an intrinsically disordered region (IDR) and a folded section. IDRs are recognized as important regions in proteins due to their roles in cellular signaling and regulation. The highly disordered segment is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif. Isozyme BnaC.DGAT1.a also exhibits positive cooperativity. The involvement of the N-terminal domain in self-association may mediate positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. The BnaDGAT1 N-terminal domain is not necessary for catalysis but contributes to modulating activity. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site. The BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction. The BnaDGAT1 N-terminal Domain is structurally flexible. The allosteric site also is needed for acyl-CoA-mediated homotropic allosteric activation	Brassica napus
physiological function	diacylglycerol acyltransferase 1 (DGAT1) is an integral membrane enzyme catalyzing the final and committed step in the acylcoenzyme A (CoA)-dependent biosynthesis of triacylglycerol (TAG). Proposed model for BnaDGAT1 regulation involving the hydrophilic N-terminal domain (NTD), overview	Brassica napus

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Release 2023.1 (January 2023)