BRENDA - Enzyme Database

Imaging the early stages of phospholipase C/sphingomyelinase activity on vesicles containing coexisting ordered-disordered and gel-fluid domains

Ibarguren, M.; Lopez, D.J.; Montes, L.R.; Sot, J.; Vasil, A.I.; Vasil, M.L.; Goni, F.M.; Alonso, A.; J. Lipid Res. 52, 635-645 (2011)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
3.1.4.3
T178A
site-directed mutagenesis, hydrolytically inactive mutant. The PlcHR 2 T178A mutant is also unable to induce vesicle aggregation or release intravesicular aqueous contents in contrast to the wild-type enzyme
Pseudomonas aeruginosa
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.4.3
Pseudomonas aeruginosa
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.4.3
additional information
activity measurement with substrate on giant unilamellar lipid vesicles. Enzyme binding to the vesicles appears to be a cooperative process and is irreversible, binding analysis using wild-type enzyme and catalytically inactive enzyme mutant T178A. After the initial cluster of bound enzyme is detected, further binding and catalytic activity follow rapidly. The enzyme preferentially binds the more disordered domains, and, in most cases, the catalytic activity causes the disordering of the other domains, at a further stage of lipid hydrolysis, lipid aggregates are formed and vesicles disintegrate, overview
715836
Pseudomonas aeruginosa
?
-
-
-
-
3.1.4.3
phosphatidylcholine + H2O
-
715836
Pseudomonas aeruginosa
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
?
3.1.4.3
phosphatidylethanolamine + H2O
-
715836
Pseudomonas aeruginosa
1,2-diacyl-sn-glycerol + ethanolamine phosphate
-
-
-
?
3.1.4.3
sphingomyelin + H2O
-
715836
Pseudomonas aeruginosa
N-acylsphingosine + choline phosphate
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.1.4.3
28
-
assay at
Pseudomonas aeruginosa
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.4.3
7.4
-
assay at
Pseudomonas aeruginosa
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.1.4.3
T178A
site-directed mutagenesis, hydrolytically inactive mutant. The PlcHR 2 T178A mutant is also unable to induce vesicle aggregation or release intravesicular aqueous contents in contrast to the wild-type enzyme
Pseudomonas aeruginosa
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.4.3
additional information
activity measurement with substrate on giant unilamellar lipid vesicles. Enzyme binding to the vesicles appears to be a cooperative process and is irreversible, binding analysis using wild-type enzyme and catalytically inactive enzyme mutant T178A. After the initial cluster of bound enzyme is detected, further binding and catalytic activity follow rapidly. The enzyme preferentially binds the more disordered domains, and, in most cases, the catalytic activity causes the disordering of the other domains, at a further stage of lipid hydrolysis, lipid aggregates are formed and vesicles disintegrate, overview
715836
Pseudomonas aeruginosa
?
-
-
-
-
3.1.4.3
phosphatidylcholine + H2O
-
715836
Pseudomonas aeruginosa
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
?
3.1.4.3
phosphatidylethanolamine + H2O
-
715836
Pseudomonas aeruginosa
1,2-diacyl-sn-glycerol + ethanolamine phosphate
-
-
-
?
3.1.4.3
sphingomyelin + H2O
-
715836
Pseudomonas aeruginosa
N-acylsphingosine + choline phosphate
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.1.4.3
28
-
assay at
Pseudomonas aeruginosa
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.4.3
7.4
-
assay at
Pseudomonas aeruginosa