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Literature summary for 3.1.4.4 extracted from
- Cloning, expression and functional characterization of the C2 domain from tomato phospholipase Dalpha (2011), Plant Physiol. Biochem., 49, 18-32.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the sequence corresponding to the N-terminal 164 amino acids of the full length cDNA of phospholipase Dalpha from tomato fruit is cloned in pET28(b) vector and expressed in Escherichia coli as a His-tagged protein, transient expression of C2-YFP | Solanum lycopersicum |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | recombinant C2 domain shows micromolar affinity towards Ca2+ with a maximum of 2 high affinity binding sites, unique calcium binding pockets with high electro-negativity | Solanum lycopersicum |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Solanum lycopersicum | interaction of PLDalpha C2 domain with synthetic unilamellar vesicles shows maximum affinity towards phosphatidic acid, and virtually no binding with phosphatidylcholine. Electrostatic, rather than a hydrophobic mode of interaction between C2 domain and the phospholipid vesicles. The binding towards phosphoinositides is reduced with increasing degree of phosphorylation | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Solanum lycopersicum | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | the C2 domain is phosphorylated. The binding towards phosphoinositides is reduced with increasing degree of phosphorylation | Solanum lycopersicum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| fruit | - |
Solanum lycopersicum | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | interaction of PLDalpha C2 domain with synthetic unilamellar vesicles shows maximum affinity towards phosphatidic acid, and virtually no binding with phosphatidylcholine. Electrostatic, rather than a hydrophobic mode of interaction between C2 domain and the phospholipid vesicles. The binding towards phosphoinositides is reduced with increasing degree of phosphorylation | Solanum lycopersicum | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| phospholipase Dalpha | - |
Solanum lycopersicum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | phospholipase Dalpha is involved in fruit development | Solanum lycopersicum |
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Release 2023.1 (January 2023)
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