Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Morasso, C.; Bellini, T.; Monti, D.; Bassi, M.; Prosperi, D.; Riva, S.
    Dispersed phantom scatterer technique reveals subtle differences in substrate recognition by phospholipase D inactive mutants (2009), ChemBioChem, 10, 639-644.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.4 Streptomyces sp. PMF
-
-
-

Reaction

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.4 PLD-PMF
-
Streptomyces sp. PMF