Skip to main content

Dopamine β-monooxygenase

  • Chapter
Springer Handbook of Enzymes

Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES,volume 27))

  • 76 Accesses

Nomenclature

EC number

1.14.17.1

Systematic name

3,4-dihydroxyphenethylamine,ascorbate:oxygen oxidoreductase (β-hydroxylating)

Recommended name

dopamine β-monooxygenase

Synonyms

3,4-dihydroxyphenethylamine β-oxidase

3,4-dihydroxyphenethylamine β-hydroxylase

4-(2-aminoethyl)pyrocatechol β-oxidase

EC 1.14.2.1 (formerly)

MDBH <1> (<1> membrane-associated dopamine β-monooxygenase [1]) [1]

SDBH <1> (<1> soluble dopamine β-monooxygenase [1]) [1]

dopa β-hydroxylase

dopamine β-hydrolase

dopamine β-hydroxylase

dopamine β-oxidase

dopamine hydroxylase

dopamine(3,4-dihydroxyphenethylamine)β-mono-oxygenase

dopamine-B-hydroxylase <1> (<1> DBH [14]) [14]

oxygenase, dopamine β-mono-phenylamine β-hydroxylase

CAS registry number

9013-38-1

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 259.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 329.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 329.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Slater, E.P.; Zaremba, S.; Hogue-Angeletti, R.A.: Purification of membrane-bound dopamine Β-monooxygenase from chromaffin granules: relation to soluble dopamine Β-monooxygenase. Arch. Biochem. Biophys., 211, 288–296 (1981)

    Article  PubMed  CAS  Google Scholar 

  2. Okuno, S.; Fujisawa, H.: Purification and characterization of rat dopamine Β-monooxygenase and monoclonal antibodies to the enzyme. Biochim. Biophys. Acta, 799, 260–269 (1984)

    PubMed  CAS  Google Scholar 

  3. Tian, G.; Berry, J.A.; Klinman, J.P.: Oxygen-18 kinetic isotope effects in the dopamine Β-monooxygenase reaction: Evidence for a new chemical mechanism in non-heme, metallomonooxygenase. Biochemistry, 33, 226–234 (1994)

    Article  PubMed  CAS  Google Scholar 

  4. Fong, J.C.; Shenkman, L.; Goldstein, M.: Purification and characterization of rat pheochromocytoma dopamine Β-hydroxylase. J. Neurochem., 34, 346–350 (1980)

    Article  PubMed  CAS  Google Scholar 

  5. Colombo, G.; Papadopoulos, N.J.; Ash, D.E.; Villafranca, J.J.: Characterization of highly purified dopamine Β-hydroxylase. Arch. Biochem. Biophys., 252, 71–80 (1987)

    Article  PubMed  CAS  Google Scholar 

  6. Frigon, R.P.; Stone, R.A.: Human plasma dopamine Β-hydroxylase. Purification and properties. J. Biol. Chem., 253, 6780–6786 (1978)

    PubMed  CAS  Google Scholar 

  7. Long, R.A.; Weppelman, R.M.; Taylor, J.E.; Tolman, R. L.; Olson, G.: Purification and characterization of avian dopamine Β-hydroxylase. Biochemistry, 20, 7423–7431 (1981)

    Article  PubMed  CAS  Google Scholar 

  8. Aunis, D.; Miras-Portugal, M.T.; Mandel, P.: Bovine adrenal medullary dopamine Β-hydroxylase: purification by affinity chromatography, kinetic studies and presence of essential histidyl residues. Biochim. Biophys. Acta, 327, 313–327 (1973)

    PubMed  CAS  Google Scholar 

  9. Merkler, D.J.; Kulathila, R.; Francisco, W.A.; Ash, D.E.; Bell, J.: The irreversible inactivation of two copper-dependent monooxygenases by sulfite: peptidylglycine α-amidating enzyme and dopamine Β-monooxygenase. FEBS Lett, 366, 165–169 (1995)

    Article  PubMed  CAS  Google Scholar 

  10. Hamos, J.; Desai, P.R.; Villafranca, J.J.: Characterization and kinetic studies of deglycosylated dopamine Β-hydroxylase. FASEB J., 1, 143–148 (1987)

    PubMed  CAS  Google Scholar 

  11. Levin, E.Y.; Levenberg, B.; Kaufman, S.: The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. J. Biol. Chem., 235, 2080–2086 (1960)

    PubMed  CAS  Google Scholar 

  12. Friedman, S.; Kaufman, S.: 3,4-dihydroxyphenylethylamine Β-hydroxylase. Physical properties, copper content, and role of copper in the catalytic acttivity. J. Biol. Chem., 240, 4763–4773 (1965)

    PubMed  CAS  Google Scholar 

  13. Rosenberg, R.C.; Gimble, J.M.; Lovenberg, W.: Inhibition of dopamine-Β-hydroxylase by alternative electron donors. Biochim. Biophys. Acta, 613, 62–72 (1980)

    PubMed  CAS  Google Scholar 

  14. May, S.W.; Mueller, P.W.; Padgette, S.R.; Herman, H. H.; Phillips, R.S.: Dopamine-B-hydroxylase: suicide inhibition by the novel olefinic substrate, 1-phenyl-1-aminomethylethene. Biochem. Biophys. Res. Commun., 110, 161–168 (1983)

    Article  PubMed  CAS  Google Scholar 

  15. Blackburn, N.J.; Collison, D.; Sutton, J.; Mabbs, F. E.: Kinetic and E.P.R. studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) Β-mono-oxygenase. Biochem. J., 220, 447–454 (1984)

    PubMed  CAS  Google Scholar 

  16. Townes, S.; Titone, C.; Rosenberg, R.C.: Inhibition of dopamine Β-hydroxylase by bidentate chelating agents. Biochim. Biophys. Acta, 1037, 240–247 (1990)

    PubMed  CAS  Google Scholar 

  17. DeWolf, W.E.; Chambers, P.A.; Southan, C.; Saunders, D.; Kruse, L.I.: Inactivation of dopamine Β-hydroxylase by Β-ethynyltyramine: kinetic characterization and covalent modification of an active site peptide. Biochemistry, 28, 3833–3842 (1989)

    Article  Google Scholar 

  18. DeWolf, W.E.; Carr, S.A.; Varrichio, A.; Goodhart, P. J.; Mentzer, M.A.; Roberts, G.D.; Southan, C.; Dolle, R.E.; Kruse, L.I.: Inactivation of dopamine Β-hydroxylase by p-cresol: isolation and characterization of covalently modified active site peptides. Biochemistry, 27, 9093–9101 (1988)

    Article  Google Scholar 

  19. Kruse, L.I.; DeWolf, W.E.; Chambers, P.A.; Goodhart, P.J.: Design and kinetic characterization of multisubstrate inhibitors of dopamine Β-hydroxylase. Biochemistry, 25, 7271–7278 (1986)

    Article  PubMed  CAS  Google Scholar 

  20. Sirimanne, S.R.; Herman, H.H.; May, S.W.: Interaction of dopamine Β-mono-oxygenase with substituted imidazoles and pyrazoles. Catalysis and inhibition. Biochem. J., 242, 227–233 (1987)

    PubMed  CAS  Google Scholar 

  21. Bossard, M.J.; Klinman, J.P.: Mechanism-based inhibition of dopamine Β-monooxygenase by aldehydes and amides. J. Biol. Chem., 261, 16421–16427 (1986)

    PubMed  CAS  Google Scholar 

  22. Colombo, G.; Rajashekhar, B.; Giedroc, D.P.; Villafranca, J.J.: Alternate substrates of dopamine Β-hydroxylase. I. Kinetic investigations of benzyl cyanides as substrates and inhibitors. J. Biol. Chem., 259, 1593–1600 (1984)

    PubMed  CAS  Google Scholar 

  23. Colombo, G.; Rajashekhar, B.; Giedroc, D.P.; Villafranca, J.J.: Mechanism-based inhibitors of dopamine Β-hydroxylase: inhibition by 2-bromo-3-(p-hydroxyphenyl)-l-propene. Biochemistry, 23, 3590–3598 (1984)

    Article  PubMed  CAS  Google Scholar 

  24. Klinman, J.P.; Krueger, M.: Dopamine Β-hydroxylase: activity and inhibition in the presence of Β-substituted phenethylamines. Biochemistry, 21, 67–75 (1982)

    Article  PubMed  CAS  Google Scholar 

  25. May, S.W.; Young, F.K.; Powers, J.L.; Gill-Woznichak, M.M.: Mechanism-based inactivation of dopamine Β-monooxygenase in adrenal chromaffin cells. Biochem. Biophys. Res. Commun., 228, 278–284 (1996)

    Article  PubMed  CAS  Google Scholar 

  26. Izumi, H.; Hayakari, M.; Kondo, Y.; Takemoto, T.: Inhibition of dopamine Β-monooxygenase by histidine. Hoppe-Seyler’s Z. Physiol. Chem., 356, 1831–1833 (1975)

    CAS  Google Scholar 

  27. Ljones, T.; Skotland, T.; Fiatmark, T.: Purification and characterization of dopamine Β-hydroxylase from bovine adrenal medulla. Eur. J. Biochem., 61, 525–533 (1976)

    Article  PubMed  CAS  Google Scholar 

  28. Skotland, T.; Ljones, T.: The enzyme-bound copper of dopamine Β-mono-oxygenase. Reaction with copper chelators, preparation of the apoprotein, and kinetics of the reconstitution by added copper. Eur. J. Biochem., 94, 145–151 (1979)

    Article  PubMed  CAS  Google Scholar 

  29. Adrio, F.; Anadon, R.; Rodriguez-Moldes, I.: Distribution of tyrosine hydroxylase (TH) and dopamine Β-hydroxylase (DBH) immunoreactivity in thcentral nervous system of two chondrostean fishes (Acipenser baeri and Huso huso). J. Comp. Neurol, 448, 280–297 (2002)

    Article  PubMed  CAS  Google Scholar 

  30. Wimalasena, K.; Dharmasena, S.; Wimalasena, D.S.; Hughbanks-Wheaton, D.K.: Reduction of dopamine Β-monooxygenase. A unified model for apparent negative cooperativity and fumarate activation. J. Biol. Chem., 271, 26032–26043 (1996)

    Article  PubMed  CAS  Google Scholar 

  31. Gibson, K.R.; Vanek, P.G.; Kaloss, W.D.; Collier, G.B.; Connaughton, J.F.; Angelichio, M.; Livi, G.P.; Fleming, P.J.: Expression of dopamine Β-hydroxylase in Drosophila Schneider 2 cells. Evidence for a mechanism of membrane binding other than uncleaved signal peptide. J. Biol. Chem., 268, 9490–9495 (1993)

    PubMed  CAS  Google Scholar 

  32. Abudu, N.; Banjaw, M.Y.; Ljones, T.: Kinetic studies on the activation of dopamine Β-monooxygenase by copper and vanadium ions. Eur. J. Biochem., 257, 622–629 (1998)

    Article  PubMed  CAS  Google Scholar 

  33. Ishida, T.; Narita, M.; Nozaki, M.; Horiike, K.: Selective cleavage and modification of the intersubunit disulfide bonds of bovine dopamine Β-mono-oxygenase: conversion of tetramer to active dimer. J. Biochem., 120, 346–352 (1996)

    PubMed  CAS  Google Scholar 

  34. Suzuki, E.; Kurata, T.; Shiabata, M.; Mori, M.; Arakawa, N.: Activities of d-and L-xyloascorbic acid and D-and L-araboascorbic acid as a cofactor for dopamine Β-hydroxylase reaction. J. Nutr. Sci. Vitaminol., 43, 491–496 (1997)

    PubMed  CAS  Google Scholar 

  35. Caroldi, S.; De Paris, P.; Zotti, S.; Zanella, I.; Brugnone, F.: Effects of disulfiram on serum dopamine-Β-hydroxylase and blood carbon disulphide concentrations in alcoholics. J. Appl. Toxicol., 14, 77–80 (1994)

    Article  PubMed  CAS  Google Scholar 

  36. De Paris, P.; Caroldi, S.: In vitro effect of dithiocarbamate pesticides and of CaNa2EDTA on human serum dopamine-Β-hydroxylase. Biomed. Environ. Sci., 8, 114–121 (1995)

    PubMed  Google Scholar 

  37. Fortin, D.; Coulon, J.E; Roberge, A.G.: Comparative study of biochemical parameters and kinetic properties of dopamine-Β-hydroxylase activity from cat and rat adrenals. Comp. Biochem. Physiol. B, 104, 567–575 (1993)

    Article  PubMed  CAS  Google Scholar 

  38. Narita, M.; Ishida, T.; Tomoyoshi, T.; Nozaki, M.; Horiike, K.: A natural variant of bovine dopamine Β-monooxygenase with phenylalanine as residue 208: purification and characterization of the variant homo-and heterotetramers of (F208)4 and (F208)2(L208)2. FEBS Lett., 396, 208–212 (1996)

    Article  PubMed  CAS  Google Scholar 

  39. Reedy, B.J.; Murthy, N.N.; Karlin, K.D.; Blackburn, N.J.: Isocyanides as ligand-directed indicators of Cu(I) coordination in copper proteins. Probing the inequivalence of the Cu(I) centers in reduced dopamine-Β-monooxygenase. J. Am. Chem. Soc., 117, 9826–9831 (1995)

    Article  CAS  Google Scholar 

  40. Prohaska, J.R.; Brokate, B.: Dietary copper deficiency alters protein levels of rat dopamine Β-monooxygenase and tyrosine monooxygenase. Exp. Biol. Med., 226, 199–207 (2001)

    CAS  Google Scholar 

  41. Feng, Z.; Sabban, E.L.: Regulation of the translation and processing of rat dopamine Β-hydroxylase by metal ions in a cell free system. Biochem. Mol. Biol. Int., 36, 339–345 (1995)

    PubMed  CAS  Google Scholar 

  42. Oyarce, A.M.; Steveson, T.C.; Jin, L.; Eipper, B.A.: Dopamine Β-monooxygenase signal/anchor sequence alters trafficking of peptidylglycine α-hydroxylating monooxygenase. J. Biol. Chem., 276, 33265–33272 (2001)

    Article  PubMed  CAS  Google Scholar 

Download references

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2006 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

(2006). Dopamine β-monooxygenase. In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 27. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-30439-8_14

Download citation

Publish with us

Policies and ethics