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Literature summary extracted from

  • Ishida, T.; Narita, M.; Nozaki, M.; Horiike, K.
    Selective cleavage and modification of the intersubunit disulfide bonds of bovine dopamine beta-monooxygenase: conversion of tetramer to active dimer (1996), J. Biochem., 120, 346-352.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.17.1 additional information
-
 additional information comparison of Km of native enzyme and dimeric and tetrameric species after treatment with dithiothreitol and iodoacetamide Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.17.1 soluble
-
 Bos taurus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.17.1 260000
-
 native enzyme, low-angle laser light scattering photometry coupled with high-performance gel filtration Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.14.17.1 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.17.1 adrenal medulla
-
 Bos taurus
-

Storage Stability

EC Number Storage Stability Organism
1.14.17.1 4°C, stable for at least several days, dimeric species Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.17.1 3,4-dihydroxyphenethylamine + ascorbate + O2
-
 Bos taurus noradrenaline + dehydroascorbate + H2O norepinephrine ?
1.14.17.1 tyramine + ascorbate + O2
-
 Bos taurus octopamine + dehydroascorbate + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.17.1 tetramer 4 * 66000-74000, SDS-PAGE after cleavage of intersubunit disulfide bonds with dithiothreitol, tetramer consists of two disulfid-linked dimers Bos taurus