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Literature summary for 2.3.1.158 extracted from
- Phospholipid:diacylglycerol acyltransferase is a multifunctional enzyme involved in membrane lipid turnover and degradation while synthesizing triacylglycerol in the unicellular green microalga Chlamydomonas reinhardtii (2012), Plant Cell, 24, 3708-3724.
Application
| Application | Comment | Organism |
|---|---|---|
| energy production | the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production | Chlamydomonas reinhardtii |
| industry | the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production | Chlamydomonas reinhardtii |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene encoding PDAT, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of full-length enzyme and of truncated PDAT lacking the transmembrane domain in Pichia pastoris | Chlamydomonas reinhardtii |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Chlamydomonas reinhardtii | 16020 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 95000 | - |
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE | Chlamydomonas reinhardtii |
| 104600 | - |
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE | Chlamydomonas reinhardtii |
| 120000 | - |
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE | Chlamydomonas reinhardtii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phospholipid + 1,2-diacyl-sn-glycerol | Chlamydomonas reinhardtii | PDAT uses membrane lipids (e.g., phospholipids and glycolipids) as the substrates for the acyl transfer reaction or hydrolysis in vivo | lysophospholipid + triacylglycerol | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chlamydomonas reinhardtii | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant full-length enzyme and truncated PDAT lacking the transmembrane domain from Pichia pastoris by affinity chromatography | Chlamydomonas reinhardtii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | PDAT shows broad substrate specificity, overview | Chlamydomonas reinhardtii | ? | - |
? | |
| phospholipid + 1,2-diacyl-sn-glycerol | PDAT uses membrane lipids (e.g., phospholipids and glycolipids) as the substrates for the acyl transfer reaction or hydrolysis in vivo | Chlamydomonas reinhardtii | lysophospholipid + triacylglycerol | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE | Chlamydomonas reinhardtii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDAT | - |
Chlamydomonas reinhardtii |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Chlamydomonas reinhardtii | sequence calculation | - |
5.96 |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Chlamydomonas reinhardtii | Cr-PDAT is transiently upregulated in response to N deprivation. The protein expression achieves the maximum level at 3 h after the onset of N depletion from the culture medium and then gradually decreases during the following 48 h | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | PDAT belongs to the LCAT-like family | Chlamydomonas reinhardtii |
| malfunction | artificial microRNA silencing of PDAT alters the membrane lipid composition, reducing the maximum specific growth rate | Chlamydomonas reinhardtii |
| physiological function | phospholipid:diacylglycerol acyltransferase in the green microalga Chlamydomonas reinhardtii catalyzes triacylglycerol synthesis via two pathways: transacylation of diacylglycerol with acyl groups from phospholipids and galactolipids and diacylglycerol:diacylglycerol transacylation. PDAT-mediated membrane lipid turnover and triacylglycerol synthesis is essential for vigorous growth under favorable culture conditions and for membrane lipid degradation with concomitant production of triacylglycerol for survival under stress. PDAT also possesses acyl hydrolase activities using triacylglycerols, phospholipids, galactolipids, and cholesteryl esters as substrates | Chlamydomonas reinhardtii |
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Release 2023.1 (January 2023)
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