Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.6 S-adenosyl-L-homocysteine
-
 Homo sapiens
2.1.1.6 tropolone
-
 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
-
 Homo sapiens
2.1.1.6 0.0031
-
 S-adenosyl-L-methionine
-
 Homo sapiens
2.1.1.6 0.0033
-
 dopamine
-
 Homo sapiens

Localization

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

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.6 brain
-
 Homo sapiens
-

Substrates and Products (Substrate)

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.1.6 0.001
-
 S-adenosyl-L-homocysteine cosubstrate S-adenosyl-L-methionine Homo sapiens
2.1.1.6 0.005
-
 tropolone plus dopamine Homo sapiens