Literature summary for 2.1.1.6 extracted from

Rutherford, K.; Alphandery, E.; McMillan, A.; Daggett, V.; Parson, W.W.
The V108M mutation decreases the structural stability of catechol O-methyltransferase (2008), Biochim. Biophys. Acta, 1784, 1098-1105.

Search for more literature for 2.1.1.6

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Homo sapiens

Protein Variants

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

General Stability	Organism
S-adenosyl-L-methionine significantly stabilizes the secondary structures of the wild type enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P21964	-	-

Purification (Commentary)

Purification (Comment)	Organism
TALON metal affinity resin column chromatography, Superdex 75 gel filtration	Homo sapiens

Synonyms

Synonyms	Comment	Organism
COMT	-	Homo sapiens

Temperature Stability [°C]

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

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Release 2023.1 (January 2023)