EC Number | Application | Comment | Organism |
---|---|---|---|
2.3.1.20 | biotechnology | WS/DGAT might have possible additional specificities, making it highly attractive for biotechnological applications such as biodiesel production | Thermomonospora curvata |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.20 | 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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.3.1.20 | membrane | - |
Thermomonospora curvata | 16020 | - |
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 | Thermomonospora curvata | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
2.3.1.20 | acyl-CoA + 1,2-diacyl-sn-glycerol | Thermomonospora curvata DSM 43183 | - |
CoA + 1,2,3-triacylglycerol | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.20 | Thermomonospora curvata | D1AD40 | - |
- |
2.3.1.20 | Thermomonospora curvata DSM 43183 | D1AD40 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.3.1.20 | additional information | strain DSM 43183 shows an optimal growing temperature of 50°C | Thermomonospora curvata | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.20 | acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Thermomonospora curvata | CoA + 1,2,3-triacylglycerol | - |
? | |
2.3.1.20 | acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Thermomonospora curvata DSM 43183 | CoA + 1,2,3-triacylglycerol | - |
? | |
2.3.1.20 | 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 | ? | - |
- |
|
2.3.1.20 | 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 | ? | - |
- |
|
2.3.1.20 | palmitoyl-CoA + 1,2-diacyl-sn-glycerol | - |
Thermomonospora curvata | CoA + 1,2-diacyl-3-palmitoyl-sn-glycerol | - |
? | |
2.3.1.20 | palmitoyl-CoA + 1,2-diacyl-sn-glycerol | - |
Thermomonospora curvata DSM 43183 | CoA + 1,2-diacyl-3-palmitoyl-sn-glycerol | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.20 | ? | x * 51720, tDGAT, sequence calculation | Thermomonospora curvata |
2.3.1.20 | 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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.20 | ACY99349 | - |
Thermomonospora curvata |
2.3.1.20 | DGAT | - |
Thermomonospora curvata |
2.3.1.20 | diacylglycerol acyltransferase | - |
Thermomonospora curvata |
2.3.1.20 | More | cf. EC 2.3.1.75 | Thermomonospora curvata |
2.3.1.20 | Tcur_3818 | - |
Thermomonospora curvata |
2.3.1.20 | tDGAT | - |
Thermomonospora curvata |
2.3.1.20 | wax ester synthase/triacylglycerol:acylCoA acyltransferase | - |
Thermomonospora curvata |
2.3.1.20 | WS/DGAT | - |
Thermomonospora curvata |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
2.3.1.20 | Thermomonospora curvata | sequence calculation | - |
6.44 |
EC Number | Organism | Comment | Expression |
---|---|---|---|
2.3.1.20 | 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 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.20 | 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 |
2.3.1.20 | additional information | three-dimensional model of the tDGAT protein, structure homology modeling | Thermomonospora curvata |