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Literature summary for 2.3.1.20 extracted from

  • Lazaro, B.; Villa, J.A.; Santin, O.; Cabezas, M.; Milagre, C.D.F.; de la Cruz, F.; Moncalian, G.
    Heterologous expression of a thermophilic diacylglycerol acyltransferase triggers triglyceride accumulation in Escherichia coli (2017), PLoS ONE, 12, e0176520 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
biotechnology WS/DGAT might have possible additional specificities, making it highly attractive for biotechnological applications such as biodiesel production Thermomonospora curvata

Cloned(Commentary)

Cloned (Comment) Organism
gene Tcur_3818, DNA and amino acid sequence determination and analysis, recombinant expression of DGAT in Escherichia coli triggering rapid triglyceride accumulation in Escherichia coli. tDGAT is associated with the lipids accumulated in recombinant Escherichia coli cells Thermomonospora curvata

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Thermomonospora curvata 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + 1,2-diacyl-sn-glycerol Thermomonospora curvata
-
CoA + 1,2,3-triacylglycerol
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol Thermomonospora curvata DSM 43183
-
CoA + 1,2,3-triacylglycerol
-
?

Organism

Organism UniProt Comment Textmining
Thermomonospora curvata D1AD40
-
-
Thermomonospora curvata DSM 43183 D1AD40
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information strain DSM 43183 shows an optimal growing temperature of 50°C Thermomonospora curvata
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + 1,2-diacyl-sn-glycerol
-
Thermomonospora curvata CoA + 1,2,3-triacylglycerol
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
-
Thermomonospora curvata DSM 43183 CoA + 1,2,3-triacylglycerol
-
?
additional information docking of palmitoyl-CoA into the donor pocket of the predicted tDGAT structure shows that the palmitoyl moiety is sandwiched between alpha5 helix and the beta sheet formed by beta9 and beta10 strands Thermomonospora curvata ?
-
-
additional information docking of palmitoyl-CoA into the donor pocket of the predicted tDGAT structure shows that the palmitoyl moiety is sandwiched between alpha5 helix and the beta sheet formed by beta9 and beta10 strands Thermomonospora curvata DSM 43183 ?
-
-
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
-
Thermomonospora curvata CoA + 1,2-diacyl-3-palmitoyl-sn-glycerol
-
?
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
-
Thermomonospora curvata DSM 43183 CoA + 1,2-diacyl-3-palmitoyl-sn-glycerol
-
?

Subunits

Subunits Comment Organism
? x * 51720, tDGAT, sequence calculation Thermomonospora curvata
More three-dimensional model of the tDGAT protein, structure homology modeling. tDGAT is predicted to have an acyl-CoA-dependent acyltransferase fold, with two domains connected by a helical linker. The core of the predicted N-terminal domain contains a four-stranded mixed sheet (beta2, beta5, beta6 and beta7) surrounded by three alpha-helices (alpha2, alpha4 and alpha5). The core of the predicted C-terminal domain consists of a five-stranded mixed sheet (beta8, beta9, beta10, beta11 and beta12) and five alpha-helices (alpha9, alpha10, alpha11, alpha13 and alpha14) covering the external face of the mixed sheet Thermomonospora curvata

Synonyms

Synonyms Comment Organism
ACY99349
-
Thermomonospora curvata
DGAT
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Thermomonospora curvata
diacylglycerol acyltransferase
-
Thermomonospora curvata
More cf. EC 2.3.1.75 Thermomonospora curvata
Tcur_3818
-
Thermomonospora curvata
tDGAT
-
Thermomonospora curvata
wax ester synthase/triacylglycerol:acylCoA acyltransferase
-
Thermomonospora curvata
WS/DGAT
-
Thermomonospora curvata

pI Value

Organism Comment pI Value Maximum pI Value
Thermomonospora curvata sequence calculation
-
6.44

Expression

Organism Comment Expression
Thermomonospora curvata successful introduction of the triacylglycerol biosynthesis pathway in gamma-proteobacteria, in an industrially appropriate microorganism, method development and optimization, overview. tDGAT is associated with the lipids accumulated in recombinant Escherichia coli cells. Optimization of fluorescence techniques for the detection of in situ TAG accumulation, Nile Red staining additional information

General Information

General Information Comment Organism
evolution Thermomonospora curvata acyltransferase ACY99349 belongs to the WS/DGAT family. tDGAT contains all the conserved motifs characteristic of WS/DGAT, mainly the catalytic site 140HHaavDG146, motif I 118PLW120, and motif II 281ND282. Like in other acyl-CoA-dependent acyltransferases the catalytic motif 140HHaavDG146, in the N-terminal domain of tDGAT, is predicted to be located in the hydrophobic pocket or channel that restricts the accessibility of hydrophilic substrates Thermomonospora curvata
additional information three-dimensional model of the tDGAT protein, structure homology modeling Thermomonospora curvata