Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | dithiothreitol treatment leads to an insignificant change in specific activity below 1% | Candida sp. (in: Saccharomycetales) |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Candida sp. (in: Saccharomycetales) |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
36000 | - |
4 * 36000, SDS-PAGE | Candida sp. (in: Saccharomycetales) |
140000 | - |
gel filtration | Candida sp. (in: Saccharomycetales) |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Candida sp. (in: Saccharomycetales) | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Candida sp. (in: Saccharomycetales) | - |
Subunits | Comment | Organism |
---|---|---|
tetramer | 4 * 36000, SDS-PAGE | Candida sp. (in: Saccharomycetales) |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the main phase of thermal inactivation follows an irreversible two-state mechanism, with loss of about 20% of the helical structure, loss of the majority of the tertiary structure, and partial exposure of tryptophan residues to solution being approximately concurrent with activity loss. This process results in the formation of aggregated molten globules. In addition, a rapid reversible denaturation phase occurs that is not completely coupled to the main phase. Enzyme inactivation is inhibited by the presence of glycerol and trimethylamine oxide. NaCl destabilizes the enzyme at elevated temperature | Candida sp. (in: Saccharomycetales) |