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Literature summary for 2.1.1.6 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
Search for more literature for 2.1.1.6

Inhibitors

Inhibitors Comment Organism Structure
S-adenosyl-L-homocysteine
-
 Homo sapiens

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

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

Substrates and Products (Substrate)

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