EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.1.1 | cetyltrimethylammonium bromide | complete inhibition | Sus scrofa | |
3.1.1.1 | dimyristoylphosphatidylcholine | 88% inhibition | Sus scrofa | |
3.1.1.1 | dipalmitoylphosphatidylcholine | 91.5% inhibition | Sus scrofa | |
3.1.1.1 | additional information | no inhibition by sodium sulfosuccinate | Sus scrofa | |
3.1.1.1 | PEG 6000 | complete inhibition | Sus scrofa | |
3.1.1.1 | Triton X-100 | 93.6% inhibition | Sus scrofa |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.1.1 | additional information | - |
additional information | enzyme kinetics, overview. Michaelis-Menten equation can be calculated from Hanes-Woolf equation | Sus scrofa | |
3.1.1.1 | 16.44 | - |
capric acid | pH 7.0, 60°C | Sus scrofa |
EC Number | Organic Solvent | Comment | Organism |
---|---|---|---|
3.1.1.1 | Acetone | pH 7.0, 60°C, 2 h, loss of 82% activity | Sus scrofa |
3.1.1.1 | benzene | pH 7.0, 60°C, 2 h, loss of 91.6% activity | Sus scrofa |
3.1.1.1 | cyclohexane | pH 7.0, 60°C, 2 h, loss of 98.7% activity | Sus scrofa |
3.1.1.1 | heptane | pH 7.0, 60°C, 2 h, complete loss of activity | Sus scrofa |
3.1.1.1 | isooctane | pH 7.0, 60°C, 2 h, completely stable | Sus scrofa |
3.1.1.1 | n-hexane | pH 7.0, 60°C, 2 h, complete loss of activity | Sus scrofa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.1.1 | Sus scrofa | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.1.1 | commercial preparation | - |
Sus scrofa | - |
3.1.1.1 | liver | - |
Sus scrofa | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.1.1 | capric acid + glycerol | PLE-catalyzed esterification of capric acid with glycerol in reverse micelles. The most suitable structure of reverse micelles is comprised of isooctane (reaction medium) and bis(2-ethylhexyl) sodium sulfosuccinate ( anionic surfactant) with 0.1 of R-value ([water]/[surfactant]) and 3.0 of G/F-value ([glycerol]/[fatty acid]) for the PLE-catalyzed esterification. PLE mainly produces 1-monocaprin without any other products (di- and/or tricaprins of subsequent reactions). The degree of esterification at equilibrium state (after 4 h from the initiation) is 62.7% under optimum conditions. Method optimization, overview | Sus scrofa | 1-monocaprin + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.1.1 | PLE | - |
Sus scrofa |
3.1.1.1 | porcine liver carboxylesterase | - |
Sus scrofa |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.1.1 | 60 | - |
- |
Sus scrofa |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.1.1 | 7 | - |
- |
Sus scrofa |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.1.1 | evolution | porcine liver carboxylesterase (PLE), with the consensus sequence motif Gly-Glu-Ser-Ala-Gly in its lipolitic active site, belongs to carboxylesterase family as a serine-type esterase | Sus scrofa |