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Literature summary for 2.1.1.6 extracted from

  • Skopec, M.M.; Dearing, M.D.
    Differential expression and activity of catechol-O-methyl transferase (COMT) in a generalist (Neotoma albigula) and juniper specialist (Neotoma stephensi) woodrat (2011), Comp. Biochem. Physiol. C, 154, 383-390.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
 catechol pH not specified in the publication, temperature not specified in the publication Neotoma albigula
0.145
-
 catechol pH not specified in the publication, temperature not specified in the publication Neotoma stephensi
0.725
-
 catechol pH not specified in the publication, temperature not specified in the publication Neotoma stephensi
0.833
-
 catechol pH not specified in the publication, temperature not specified in the publication Neotoma albigula

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Neotoma stephensi 16020
-
soluble
-
 Neotoma stephensi
-
-

Organism

Organism UniProt Comment Textmining
Neotoma albigula
-
-
-
Neotoma stephensi
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Neotoma stephensi
-
kidney
-
 Neotoma albigula
-
liver
-
 Neotoma stephensi
-
liver
-
 Neotoma albigula
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
catechol + S-adenosyl-L-methionine
-
 Neotoma stephensi guaiacol + S-adenosyl-L-homocysteine
-
 ?
catechol + S-adenosyl-L-methionine
-
 Neotoma albigula guaiacol + S-adenosyl-L-homocysteine
-
 ?

Synonyms

Synonyms Comment Organism
catechol-O-methyl transferase
-
 Neotoma stephensi
catechol-O-methyl transferase, membrane bound
-
 Neotoma albigula
catechol-O-methyl transferase, soluble
-
 Neotoma albigula