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Literature summary extracted from

  • Gulliver, P.A.; Tipton, K.F.
    The purification and properties of pig-liver catechol-O-methyl transferase (1978), Eur. J. Biochem., 88, 439-444.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.1.1.6 complete loss of activity on freezing solid Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.6 0.056
-
 S-adenosyl-L-methionine cosubstrate 3,4-dihydroxyphenylacetic acid Sus scrofa
2.1.1.6 0.64
-
 3,4-dihydroxyphenylacetic acid
-
 Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.6 23000
-
 gel filtration Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.6 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.6 liver
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.1.6 additional information
-
-
 Sus scrofa

Storage Stability

EC Number Storage Stability Organism
2.1.1.6 -5°C, 20% v/v glycerol, stable for 6 months Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.6 3,4-dihydroxyphenylacetic acid + S-adenosyl-L-methionine
-
 Sus scrofa S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.6 additional information benzimidazole Sus scrofa ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.6 monomer 1 * 23000, SDS-PAGE Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.6 7.1 7.4
-
 Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.1.6 6.8 8 about 50% of maximum activity at pH 6.8 and pH 8 Sus scrofa