Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.20 extracted from

  • Caldo, K.M.P.; Shen, W.; Xu, Y.; Hanley-Bowdoin, L.; Chen, G.; Weselake, R.J.; Lemieux, M.J.
    Diacylglycerol acyltransferase 1 is activated by phosphatidate and inhibited by SnRK1-catalyzed phosphorylation (2018), Plant J., 96, 287-299 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
16:0/16:0-phosphatidic acid activated the enzyme by about 1.24fold Brassica napus
16:0/18:1-phosphatidic acid activates BnaDGAT1 by 2.4fold Brassica napus
18:1/18:1-phosphatidic acid activates BnaDGAT1 by 4.7fold Brassica napus
phosphatidic acid PA, Feed-forward activation of BnaDGAT1 by phosphatidate, PA facilitates the transition of the enzyme into the more active state. PA may also relieve possible autoinhibition of BnaDGAT1 brought about by the N-terminal regulatory domain, which is shown to interact with PA. The soluble domain of BnaDGAT1 is likely to interact with the small highly charged head group of PA. 18:1/18:1-PA and 16:0/18:1-PA activated BnaDGAT1 by about 4.7fold and 2.4fold, respectively. 16:0/16:0-PA only activates the enzyme by about 1.24fold, while 18:0/18:0-PA has a minimal effect on enzyme activity. Truncated enzyme BnaDGAT11-113, comprising the N-terminus, interacts with increasing amounts of PA, allowing the soluble domain to be recovered together with the liposomes upon centrifugation Brassica napus

Cloned(Commentary)

Cloned (Comment) Organism
gene DGAT1, BnaDGAT1 is recombinantly expressed using a codon-optimized cDNA in Saccharomyces cerevisiae strain H1246 microsomes, recombinant expression of truncated enzyme mutants in Saccharomyces cerevisiae strain H1246 microsomes Brassica napus

Protein Variants

Protein Variants Comment Organism
additional information construction of truncated enzyme versions, BnaDGAT11-113 and BnaDGAT181-501. Yeast transformed with BnaDGAT181-501 with N-terminal Nub tag and SnRK1 with N-terminal Cub tag grew on selective media. Truncated enzyme BnaDGAT11-113, comprising the N-terminus, interacts with increasing amounts of PA, allowing the soluble domain to be recovered together with the liposomes upon centrifugation Brassica napus

Inhibitors

Inhibitors Comment Organism Structure
additional information phosphorylation downregulates the activity of the enzyme Brassica napus
oleoyl-CoA BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition. BnaDGAT1 is less susceptible to substrate inhibition at 0.005-0.020 mM oleoyl-CoA in the presence of 1 mg/ml BSA Brassica napus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis of lipidated BnaDGAT1. BnaDGAT1 exhibits cooperative substrate binding behavior with oleoyl-CoA Brassica napus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
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 Q9XGR5
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein BnaDGAT1 has a predicted SnRK1 phosphorylation site that appears to be conserved among plant DGAT1s. This site is localized in the cytosolic loop connecting the second and third predicted transmembrane segments in the TMHMM topology, indicating that it is accessible to cytoplasmic kinases. In vitro SnRK1-catalyzed phosphorylation of BnaDGAT1 results in a decrease in BnaDGAT1 activity Brassica napus

Purification (Commentary)

Purification (Comment) Organism
recombinant BnaDGAT1 from Saccharomyces cerevisiae strain H1246 microsomes, purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-beta-D-maltopyranoside micelles is lipidated to form mixed micelles Brassica napus

Source Tissue

Source Tissue Comment Organism Textmining
cell suspension culture microspore-derived cell suspension cultures Brassica napus
-

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 relative increase in activity of microsomal BnaDGAT1, BnaDGAT181-501, and BnaDGAT2 at different concentrations of oleoyl-CoA upon addition of 18:1/18:1-phosphatidate in the reaction mixture. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA, kinetics, overview Brassica napus ?
-
-
oleoyl-CoA + 1,2-diacyl-sn-glycerol BnaDGAT1 exhibits cooperative substrate binding behavior with oleoyl-CoA. The lipidated BnaDGAT1 exhibited a sigmoidal response to increasing concentrations of oleoyl-CoA Brassica napus CoA + 1,2-diacyl-3-oleoyl-sn-glycerol
-
?

Synonyms

Synonyms Comment Organism
BnaDGAT1
-
Brassica napus
diacylglycerol acyltransferase 1
-
Brassica napus

General Information

General Information Comment Organism
metabolism diacylglycerol acyltransferase 1 (DGAT1) catalyzes the final and committed step in the Kennedy pathway for triacylglycerol (TAG) biosynthesis Brassica napus
additional information purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-beta-D-maltopyranoside micelles is lipidated to form mixed micelles. The degree of mixed micelle fluidity appears to influence acyltransferase activity. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition indicating that PA facilitates the transition of the enzyme into the more active state. PA is a key effector modulating lipid homeostasis, in addition to its well recognized role in lipid signaling Brassica napus