Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21 (DE3) cells | Pyrococcus furiosus |
Protein Variants | Comment | Organism |
---|---|---|
biofuel | the high organic solvent stability and thermal stability suggest that this enzyme may have useful biodiesel-related applications | Pyrococcus furiosus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
phenylmethylsulfonyl fluoride | remarkable reduction in activity at 1 mM | Pyrococcus furiosus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28000 | - |
recombinant protein, approximately 28000-29000 Da, SDS-PAGE | Pyrococcus furiosus |
31980 | - |
recombinant protein, MALDI-TOF spectrometry | Pyrococcus furiosus |
32040 | - |
recombinant protein, calculated from amino acid sequence | Pyrococcus furiosus |
82000 | - |
dynamic light scattering | Pyrococcus furiosus |
Organic Solvent | Comment | Organism |
---|---|---|
acetonitrile | over 50% activity is retained at 70°C in the presence of 25% (v/v) acetonitrile | Pyrococcus furiosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | Q8U3I6 | - |
- |
Purification (Comment) | Organism |
---|---|
Ni-NTA affinity column chromatography | Pyrococcus furiosus |
Renatured (Comment) | Organism |
---|---|
through heating at 80°C for 30 min in the presence of 6 M Gdm-HCl and 1 M NaCl | Pyrococcus furiosus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl acetate + H2O | - |
Pyrococcus furiosus | 4-nitrophenol + acetate | - |
? | |
4-nitrophenyl butyrate + H2O | - |
Pyrococcus furiosus | 4-nitrophenol + butyrate | - |
? | |
4-nitrophenyl palmitate + H2O | - |
Pyrococcus furiosus | 4-nitrophenol + palmitate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer or trimer | in aqueous solution, dynamic light scattering | Pyrococcus furiosus |
Synonyms | Comment | Organism |
---|---|---|
putative lysophospholipase | the enzyme is confirmed to be an esterase and also shown to be a lipase (hydrolyzing 4-nitrophenyl palmitate), with lipolytic activity being overall about 18 to 20fold lower than esterase activity | Pyrococcus furiosus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
using 4-nitrophenyl palmitate as a substrate, for a fixed pH of 8.0 | Pyrococcus furiosus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 80 | - |
Pyrococcus furiosus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | 95 | the lysophospholipase begins to unfold only above 85°C, with unfolding remaining incomplete even at 95°C | Pyrococcus furiosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
using 4-nitrophenyl palmitate as a substrate, for a fixed temperature at 70°C | Pyrococcus furiosus |