EC 1.14.17.1 - Dopamine β-monooxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.17.1

Names

Accepted name:
dopamine β-monooxygenase
Other names:
(3,4-dihydroxyphenethylamine)β-monooxygenase
3,4-dihydroxyphenethylamine β-oxidase
4-(2-aminoethyl)pyrocatechol β-oxidase
MDBH (membrane-associated dopamine β-monooxygenase)
SDBH (soluble dopamine β-monooxygenase)
dopa β-hydroxylase
dopamine β-hydroxylase
dopamine β-oxidase
dopamine hydroxylase
dopamine-B-hydroxylase
phenylamine β-hydroxylase
Systematic name:
3,4-dihydroxyphenethylamine,ascorbate:oxygen oxidoreductase (β-hydroxylating)

Reaction

Cofactor

Comments:

A copper protein. The enzyme, found in animals, binds two copper ions with distinct roles during catalysis. Stimulated by fumarate. Formerly EC 1.14.2.1.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00080
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004500
CAS Registry Number: 9013-38-1
UniProtKB/Swiss-Prot:

References

  1. Friedman, S. and Kaufman, S.
    3,4-Dihydroxyphenylethylamine β-hydroxylase. Physical properties, copper content, and role of copper in the catalytic activity.
    J. Biol. Chem. 240 : 4763-4773 (1965). [PMID: 5846992]
  2. Levin, E.Y., Levenberg, B. and Kaufman, S.
    The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine.
    J. Biol. Chem. 235 : 2080-2086 (1960). [PMID: 14416204]
  3. Skotland, T., Ljones, T.
    Direct spectrophotometric detection of ascorbate free radical formed by dopamine beta-monooxygenase and by ascorbate oxidase.
    Biochim. Biophys. Acta 630 : 30-35 (1980). [PMID: 7388045]
  4. Rahim, Z., Ali, A., Kay, B. A.
    Prevalence of Plesiomonas shigelloides among diarrhoeal patients in Bangladesh.
    Eur. J. Epidemiol. 8 : 753-756 (1992). [PMID: 1296610]

[EC 1.14.17.1 created 1965 as EC 1.14.2.1, transferred 1972 to EC 1.14.17.1]