Cloned (Comment) | Organism |
---|---|
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain M15 | Geobacillus kaustophilus |
Protein Variants | Comment | Organism |
---|---|---|
M224L | site-directed mutagenesis, the mutant enzyme shows similar oxidative stability with H2O2 as the wild-type enzyme | Geobacillus kaustophilus |
M282L | site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity compared to the wild-type enzyme | Geobacillus kaustophilus |
M285L | site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity compared to the wild-type enzyme | Geobacillus kaustophilus |
M289L | site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity compared to the wild-type enzyme | Geobacillus kaustophilus |
M299L | site-directed mutagenesis, the mutant enzyme shows increased oxidative stability with H2O2 compared to the wild-type enzyme | Geobacillus kaustophilus |
M321L | site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity and reduced oxidative stability with H2O2 compared to the wild-type enzyme | Geobacillus kaustophilus |
M400L | site-directed mutagenesis, the mutant enzyme shows 191% increased activity and increased catalytic efficiency compared to the wild-type enzyme | Geobacillus kaustophilus |
M426L | site-directed mutagenesis, the mutant enzyme shows 79% increased activity and increased catalytic efficiency compared to the wild-type enzyme | Geobacillus kaustophilus |
M445L | site-directed mutagenesis, the mutant enzyme shows 313% increased activity and increased catalytic efficiency compared to the wild-type enzyme | Geobacillus kaustophilus |
M485L | site-directed mutagenesis, the mutant enzyme shows 103% increased activity and increased catalytic efficiency compared to the wild-type enzyme | Geobacillus kaustophilus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
H2O2 | the enzyme is sensitive against oxidative damage by H2O2 | Geobacillus kaustophilus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of wild-type and methionine mutant enzymes, overview | Geobacillus kaustophilus | |
2.1 | - |
L-Leu-4-nitroanilide | pH 8.0, 55°C, recombinant wild-type enzyme | Geobacillus kaustophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus kaustophilus | - |
- |
- |
Oxidation Stability | Organism |
---|---|
the enzyme is sensitive against oxidative damage by H2O2 | Geobacillus kaustophilus |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity chromatography | Geobacillus kaustophilus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
91.6 | - |
purified recombinant wild-type enzyme | Geobacillus kaustophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Leu-4-nitroanilide + H2O | - |
Geobacillus kaustophilus | L-Leu + 4-nitroaniline | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LAP | - |
Geobacillus kaustophilus |
leucine aminopeptidase | - |
Geobacillus kaustophilus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
assay at | Geobacillus kaustophilus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
6.31 | - |
L-Leu-4-nitroanilide | pH 8.0, 55°C, recombinant wild-type enzyme | Geobacillus kaustophilus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Geobacillus kaustophilus |