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Literature summary extracted from

  • Lotta, T.; Vidgren, J.; Tilgmann, C.; Ulmanen, I.; Melen, K.; Julkunen, I.; Taskinen, J.
    Kinetics of human soluble and membrane-bound catechol O-methyltransferase: A revised mechanism and description of the thermolabile variant of the enzyme (1995), Biochemistry, 34, 4202-4210.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.6 S-adenosyl-L-homocysteine
-
 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.6 additional information
-
 additional information kinetics and mechanism Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.6 Homo sapiens
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.6 S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol mechanism Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.6 3,4-dihydroxybenzoic acid + S-adenosyl-L-methionine
-
 Homo sapiens S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.6 dopa + S-adenosyl-L-methionine
-
 Homo sapiens S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.6 dopamine + S-adenosyl-L-methionine
-
 Homo sapiens S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.6 noradrenaline + S-adenosyl-L-methionine
-
 Homo sapiens S-adenosyl-L-homocysteine + ?
-
 ?