EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.4.4 | expression of PLD-PMF in Escherichia coli in a soluble and active form | Streptomyces sp. PMF |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.4.4 | H167N | site-directed mutagenesis of a catalytic residue, the activity of the variant is completely lost even if the protein does not present any significant structural modification | Streptomyces sp. PMF |
3.1.4.4 | H440N | site-directed mutagenesis of a catalytic residue, the activity of the variant is completely lost even if the protein does not present any significant structural modification | Streptomyces sp. PMF |
3.1.4.4 | K169S | site-directed mutagenesis of a catalytic residue, the activity of the variant is completely lost even if the protein does not present any significant structural modification | Streptomyces sp. PMF |
3.1.4.4 | K442S | site-directed mutagenesis of a catalytic residue, the activity of the variant is completely lost even if the protein does not present any significant structural modification | Streptomyces sp. PMF |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.4 | phosphatidylcholine + H2O | Streptomyces sp. PMF | - |
choline + phosphatidic acid | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.4.4 | Streptomyces sp. PMF | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.1.4.4 | a phosphatidylcholine + H2O = choline + a phosphatidate | general reaction mechanism through an SN2-type associative pathway for phospholipase D-catalyzed hydrolysis of phospholipids, the formation of the phosphohistidine intermediate involves the conserved histidine 167 of the N-terminal HKD domain, overview | Streptomyces sp. PMF |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.4.4 | 4.2 | - |
substrate lysophosphatidylcholine | Streptomyces sp. PMF |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.4 | lysophosphatidylcholine + H2O | - |
Streptomyces sp. PMF | choline + lysophosphatidic acid | - |
? | |
3.1.4.4 | additional information | application of the dispersed phantom scatterer technique, which allows qualitatively and quantitatively evaluation of substrate recognition by inactivated PLD-PMF mutants, dissociation constants between different PLD mutants and LPC/C12E5-coated phantom nanoparticles, C12E5 is a commercial surfactant, n-pentaethylene glycol monododecyl ether, method evaluation, overview | Streptomyces sp. PMF | ? | - |
? | |
3.1.4.4 | phosphatidylcholine + H2O | - |
Streptomyces sp. PMF | choline + phosphatidic acid | - |
? | |
3.1.4.4 | phosphatidylcholine + H2O | essential role for catalysis of histidines 167 and 440 and lysines 169 and 442 of the two highly conserved HKD domains. H167 acts as the nucleophile by attacking the phosphorus atom of the phospholipidic substrates, while the conserved histidine of the C-terminal HKD domain, H440, plays a complementary role in the catalytic mechanism | Streptomyces sp. PMF | choline + phosphatidic acid | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.4.4 | PLD-PMF | - |
Streptomyces sp. PMF |