Cloned (Comment) | Organism |
---|---|
expressed in Pichia pastoris strain X33 | Meleagris gallopavo |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
sodium deoxycholate | recombinant and native enzymes are partially inhibited by the sodium deoxycholate and retain respectively 30 and 25% of their activities at 8 mM | Meleagris gallopavo |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | in the absence of CaCl2, the recombinant and native enzymes retain about 10% of their activities. The maximal enzyme activity is measured at 0.5 mM CaCl2 | Meleagris gallopavo |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
x * 50000, recombinant enzyme, SDS-PAGE | Meleagris gallopavo |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Meleagris gallopavo | - |
turkey | - |
Purification (Comment) | Organism |
---|---|
ammonium sulfate precipitation, DEAE cellulose column chromatography, Sephacryl S200 gel filtration, Q-Sepharose column chromatography, and Sephadex G100 gel filtration | Meleagris gallopavo |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
pancreas | - |
Meleagris gallopavo | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
399 | - |
recombinant enzyme from supernatant, using olive oil as substrate, at pH 8.5, 37°C | Meleagris gallopavo |
5300 | - |
recombinant enzyme after 13.28fold purification, using olive oil as substrate, at pH 8.5, 37°C | Meleagris gallopavo |
9500 | - |
recombinant enzyme after 13.28fold purification, using tributyrin as substrate, at pH 8.5, 37°C | Meleagris gallopavo |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme exhibits efficient hydrolysis of oilive oil in the absence of colipase and bile salts | Meleagris gallopavo | ? | - |
? | |
tributyrin + H2O | best substrate, efficient hydrolysis in the absence of colipase and bile salts | Meleagris gallopavo | dibutyrin + butyrate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 50000, recombinant enzyme, SDS-PAGE | Meleagris gallopavo |
Synonyms | Comment | Organism |
---|---|---|
TPL | - |
Meleagris gallopavo |
triacylglycerol acylhydrolase | - |
Meleagris gallopavo |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
recombinant enzyme | Meleagris gallopavo |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
at 55°C, the recombinant and native enzyme keep 75% and 85% of their activity respectively. Up to 55°C, the two enzymes retain only 10% of their activities | Meleagris gallopavo |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | 60 | the recombinant and native enzymes retain 80% and 95% of their activity, respectively, after 30 min of incubation at 50°C. At temperature over 55°C, the activity decreaseds dramatically to reach 15 to 20% for both enzymes at 60°C | Meleagris gallopavo |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
recombinant enzyme | Meleagris gallopavo |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
8 | 9 | the recombinant and native enzymes keep 100% of their activity after 30 min incubation at pH 8.0 and 9.0. When incubated at pH 3, both enzymes retain 70% of their activities | Meleagris gallopavo |