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Literature summary for 1.14.17.1 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
Search for more literature for 1.14.17.1

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Bos taurus
-
-

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
adrenal medulla
-
 Bos taurus
-

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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