EC Number   |
Protein Variants |
Reference |
|---|
    4.1.99.1 | analysis |
the metabolic enzyme tryptophanase (TPase) is used for biosensor construction, TPase is biotinylated so that it can be coupled with a molecular recognition element, such as an antibody, to develop an ELISA-like assay. This method is used for the detection of an antibody present in nM concentrations by the human nose. TPase can also be combined with the enzyme pyridoxal kinase (PKase) for use in a coupled assay to detect adenosine 5'-triphosphate (ATP). When ATP is present in the low mM concentration range, the coupled enzymatic system generates an odor that is easily detectable by the human nose. Biotinylated TPase can be combined with various biotinlabeled molecular recognition elements, thereby enabling a broad range of applications for this odor-based reporting system |
746742 |
| 4.1.99.1 | C298S |
the mutant displays reduced activity, subsequent to incubation at 2°C, the mutant Trpase loses about 90% of its activity |
-, 702931 |
| 4.1.99.1 | C352A/Q353A/Q354A |
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase |
747414 |
| 4.1.99.1 | D133A |
site-directed mutagenesis, inactive mutant |
747245 |
| 4.1.99.1 | D137A |
site-directed mutagenesis, inactive mutant |
-, 746778 |
| 4.1.99.1 | D363A/K366A |
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity |
747414 |
| 4.1.99.1 | D404A |
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity |
747414 |
| 4.1.99.1 | D42A/S43A/E44A/D45A |
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase |
747414 |
| 4.1.99.1 | D49A/T52A/D53A/S54A |
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase |
747414 |
| 4.1.99.1 | E17A/K20A/R21A |
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity |
747414 |
