Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
V108M | the mutation decreases the structural stability of catechol O-methyltransferase, the mutant loses enzymatic activity more rapidly than the wild type enzyme at physiological temperature, the midpoint of the thermal transition of V108M is 5-7°C lower than that of wild type enzyme, and the free energy of unfolding at 25°C is smaller by about 0.4 kcal/mol, the mutant also iss more prone to aggregation or partial unfolding to a form with an increased radius of hydration at 37°C. The mutation is associated with increased risk of breast cancer and several neuropsychiatric disorders, | Homo sapiens |
General Stability | Organism |
---|---|
S-adenosyl-L-methionine significantly stabilizes the secondary structures of the wild type enzyme | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P21964 | - |
- |
Purification (Comment) | Organism |
---|---|
TALON metal affinity resin column chromatography, Superdex 75 gel filtration | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
COMT | - |
Homo sapiens |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | 60 | wild type soluble COMT loses most of the native helical structure in a sharp melting transition between 50 and 60°C | Homo sapiens |