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Literature summary for 2.1.1.6 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
Search for more literature for 2.1.1.6

General Stability

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1 7.4
-
 Sus scrofa

pH Range

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