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Literature summary for 2.1.1.6 extracted from

  • Rivett, A.J.; Roth, J.A.
    Kinetic studies on the O-methylation of dopamine by human brain membrane-bound catechol O-methyltransferase (1982), Biochemistry, 21, 1740-1742.
    View publication on PubMed
Search for more literature for 2.1.1.6

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Homo sapiens
0.0031
-
 S-adenosyl-L-methionine
-
 Homo sapiens
0.0033
-
 dopamine
-
 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Homo sapiens 16020
-

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 ordered reaction mechanism with S-adenosyl-L-methionine as the leading substrate Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dopamine + S-adenosyl-L-methionine
-
 Homo sapiens S-adenosyl-L-homocysteine + ?
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.001
-
 S-adenosyl-L-homocysteine cosubstrate S-adenosyl-L-methionine Homo sapiens
0.005
-
 tropolone plus dopamine Homo sapiens