Literature summary for 3.1.4.4 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.

Search for more literature for 3.1.4.4

Cloned(Commentary)

Cloned (Comment)	Organism
expression of PLD-PMF in Escherichia coli in a soluble and active form	Streptomyces sp. PMF

Protein Variants

Protein Variants	Comment	Organism
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
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
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
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
phosphatidylcholine + H2O	Streptomyces sp. PMF	-	choline + phosphatidic acid	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptomyces sp. PMF	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
4.2	-	substrate lysophosphatidylcholine	Streptomyces sp. PMF

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
lysophosphatidylcholine + H2O	-	Streptomyces sp. PMF	choline + lysophosphatidic acid	-	?
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	?	-	?
phosphatidylcholine + H2O	-	Streptomyces sp. PMF	choline + phosphatidic acid	-	?
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

Synonyms	Comment	Organism
PLD-PMF	-	Streptomyces sp. PMF

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)