Cloned (Comment) | Organism |
---|---|
the His6-containing isatin hydrolase isoform b is expressed in Eschertichia coli BL21 AI cells | Roseibium aggregatum |
Crystallization (Comment) | Organism |
---|---|
crystal structures of isatin hydrolase from Labrenzia aggregata in the apo and the product state. Apo-isatin hydrolase isoform b is crystallized by vapor diffusion using sitting drop trays with a protein concentration of 20 mg/ml. Crystals appear in 0.2 M calcium acetate, 16% (w/v) PEG3350, and 1 mM MnCl2 and grew within 48 h | Roseibium aggregatum |
Protein Variants | Comment | Organism |
---|---|---|
S225A | no significant difference in Km or kcat/Km is observed between wild-type enzyme and mutant enzyme. Decrease in melting temperature of 2°C, as compared to wild-type enzyme | Roseibium aggregatum |
S225C | the S225C mutant is catalytically activated by the mutation. the biophysical properties of the of the wt and S225C enzyme appear unchanged | Roseibium aggregatum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
thioisatinate | - |
Roseibium aggregatum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Roseibium aggregatum | A0NLY7 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Roseibium aggregatum |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
51 | - |
melting temperature of mutant enzyme S225A | Roseibium aggregatum |
53 | - |
melting te,perature of wild-type enzyme and mutant enzyme S225C | Roseibium aggregatum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Roseibium aggregatum |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.01 | - |
thioisatinate | pH 8.0, temperature not specified in the publication | Roseibium aggregatum |