EC Number | Protein Variants | Comment | 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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
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EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.4.3 | Pseudomonas aeruginosa | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | Pseudomonas aeruginosa | ? | - |
? | |
3.1.4.3 | phosphatidylcholine + H2O | - |
Pseudomonas aeruginosa | 1,2-diacyl-sn-glycerol + choline phosphate | - |
? | |
3.1.4.3 | phosphatidylethanolamine + H2O | - |
Pseudomonas aeruginosa | 1,2-diacyl-sn-glycerol + ethanolamine phosphate | - |
? | |
3.1.4.3 | sphingomyelin + H2O | - |
Pseudomonas aeruginosa | N-acylsphingosine + choline phosphate | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.4.3 | 28 | - |
assay at | Pseudomonas aeruginosa |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.4.3 | 7.4 | - |
assay at | Pseudomonas aeruginosa |