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Literature summary for 2.1.1.6 extracted from

  • Bertocci, B.; Garotta, G.; Da Prada, M.; Lahm, H.W.; Zurcher, G.; Virgallita, G.; Miggiano, V.
    Immunoaffinity purification and partial amino acid sequence analysis of catechol-O-methyltransferase from pig liver (1991), Biochim. Biophys. Acta, 1080, 103-109.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane exists in a soluble cytosolic and in a particulate membrane-bound form Homo sapiens 16020
-
membrane exists in a soluble cytosolic and in a particulate membrane-bound form Sus scrofa 16020
-
microsome
-
Homo sapiens
-
-
microsome
-
Sus scrofa
-
-
soluble exists in a soluble cytosolic and in a particulate membrane-bound form Homo sapiens
-
-
soluble exists in a soluble cytosolic and in a particulate membrane-bound form Sus scrofa
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
x * 29000, hepatoma cell line G2, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
hepatoma cell line G2
-
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
soluble form Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
Hep-G2 cell
-
Homo sapiens
-
liver
-
Homo sapiens
-
liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Homo sapiens
additional information
-
-
Sus scrofa

Subunits

Subunits Comment Organism
? x * 29000, hepatoma cell line G2, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
MB-COMT membrane-bound form of catechol-O-methyltransferase Homo sapiens
MB-COMT membrane-bound form of catechol-O-methyltransferase Sus scrofa
S-COMT soluble form of catechol-O-methyltransferase Homo sapiens
S-COMT soluble form of catechol-O-methyltransferase Sus scrofa