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Literature summary for 2.3.1.20 extracted from
- Characterization and engineering of a dual-function diacylglycerol acyltransferase in the oleaginous marine diatom Phaeodactylum tricornutum (2018), Biotechnol. Biofuels, 11, 32 .
Application
| Application | Comment | Organism |
|---|---|---|
| biofuel production | PtWS/DGAT is a bifunctional enzyme and may serve as a promising target for the engineering of microalga-based oils and waxes for industrial use | Phaeodactylum tricornutum |
| industry | PtWS/DGAT is a bifunctional enzyme and may serve as a promising target for the engineering of microalga-based oils and waxes for industrial use | Phaeodactylum tricornutum |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| quantitative PCR expression analysis of PtDGATX, comparison of isozyme transcription levels and dynamics | Phaeodactylum tricornutum |
| quantitative PCR expression analysis of PtDGATX, comparison of isozyme transcription levels and dynamics, gene expression analysis, functional recombinant expression of His6-tagged DGATX using promoters of fcpA and fcpB genes (and fcpA terminators) in Saccharomyces cerevisiae strain H1246 that is deficient in TAG biosynthesis, a substantial amount of wax ester is detected in H1246-PtDGAT, indicating the dual function of PtDGATX. Endogenous overexpression of PtWS/DGAT. In H1246-PtWS/DGAT, TAG and wax ester account for 10.51 and 5.17%, respectively, of the total lipids. C16:1 and C18:1 are the dominant fatty acid species in total lipids, fatty acid content of total lipid in Saccharomyces cerevisiae, overview | Phaeodactylum tricornutum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Phaeodactylum tricornutum | 16020 | - |
| membrane | a transmembrane enzyme | Phaeodactylum tricornutum | 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 | Phaeodactylum tricornutum | - |
CoA + triacylglycerol | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Phaeodactylum tricornutum | - |
unicellular microalga | - |
| Phaeodactylum tricornutum | G4WK06 | unicellular microalga | - |
| Phaeodactylum tricornutum | I6QM80 | unicellular microalga | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Phaeodactylum tricornutum | CoA + triacylglycerol | - |
? | |
| additional information | in vitro and in vivo assays reveals that PtWS/DGAT, functioning as either a wax synthase (WS) or a diacylglycerol acyltransferase (DGAT), exhibits a preference on saturated fatty acid substrate | Phaeodactylum tricornutum | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acyl-CoA:diacylglycerol acyltransferase | - |
Phaeodactylum tricornutum |
| DGAT | - |
Phaeodactylum tricornutum |
| DGAT1 | - |
Phaeodactylum tricornutum |
| DGAT2b | - |
Phaeodactylum tricornutum |
| dual-function diacylglycerol acyltransferase | - |
Phaeodactylum tricornutum |
| More | cf. EC 2.3.1.75 | Phaeodactylum tricornutum |
| PtDGATX | - |
Phaeodactylum tricornutum |
| PtWS/DGAT | - |
Phaeodactylum tricornutum |
| WS/DGAT | - |
Phaeodactylum tricornutum |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Phaeodactylum tricornutum | the three PtDGAT genes are all upregulated under nitrogen (N)-depleted conditions, although the expression patterns of the individual DGATs are markedly different. PtDGAT1 shows transient upregulation, with its transcript levels peaking at 1 day following the onset of N depletion and declining slightly thereafter | up |
| Phaeodactylum tricornutum | the three PtDGAT genes are all upregulated under nitrogen (N)-depleted conditions, although the expression patterns of the individual DGATs are markedly different. The transcript levels of PtDGATX increases more slowly and continuously, peaking at 4 days. Engineering PtWS/DGAT for increased lipid productivity, overview. Combined with the elevated lipid and TAG content, the genetically modified Phaeodactylum tricornutum cells are quite capable of photoautotrophic growth, absorbing CO2 and producing (especially) biomass, lipids, and TAG | up |
| Phaeodactylum tricornutum | the three PtDGAT genes were all upregulated under nitrogen (N)-depleted conditions, although the expression patterns of the individual DGATs were markedly different. Isozyme PtDGAT2B exhibits the greatest fold change (20.3fold). Upregulation of PtDGAT2B occurs rapidly within the first day upon N-depletion and remains at a relatively constant level thereafter | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | in Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGA T3s | Phaeodactylum tricornutum |
| evolution | in Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGAT3s | Phaeodactylum tricornutum |
| evolution | the principal activity of DGATs has been defined as a single-function enzyme catalyzing the esterification of diacylglycerol with acyl-CoA. A dual-function PtWS/DGAT associated with diatom Phaeodactylum tricornutum is discovered in the current study. Distinctive to documented microalgal DGAT types, PtWS/DGAT exhibits activities of both a wax ester synthase (WS) and a DGAT. WS/DGATs are broadly distributed in microalgae, with different topology and phylogeny from those of DGAT1s, DGAT2s, and DGAT3s. In Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGA T3s | Phaeodactylum tricornutum |
| malfunction | overexpression of PtWS/DGAT in the diatom results in increased levels of total lipids (TL) and triacylglycerol (TAG) regardless of nitrogen availability | Phaeodactylum tricornutum |
| metabolism | acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis | Phaeodactylum tricornutum |
| metabolism | acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis. PtDGAT2B gene may contribute more to TAG synthesis in the early stage than during the later stages | Phaeodactylum tricornutum |
| metabolism | acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis. PtDGATX gene may contribute more to TAG synthesis in the later stage than during the earlier stages | Phaeodactylum tricornutum |
| physiological function | regardless of N availability, PtWS/DGAT exhibits a DGAT activity with a preference on saturated fatty acids. PtWS/DGAT exhibits activities of both a wax ester synthase (WS, EC 2.3.1.75) and a diacylglycerol acyltransferase (DGAT, EC 2.3.1.20) | Phaeodactylum tricornutum |
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