Skip to main content

3-Substituted-4-methoxy-5-hydroxybenzaldehydes and benzoic acids as inhibitors of catechol-O-methyltransferase

  • Chapter
Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects

Abstract

The extraneuronal inactivation of catecholamines and the detoxification of many xenobiotic catechols are dependent upon the enzyme catechol-O-methyltransferase (COMT, EC 2.1.1.6). COMT is a soluble, magnesium-requiring enzyme which catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to a catechol substrate resulting in the formation of the meta and para-O-methylated products (Borchardt, 1980).

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 89.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever

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

  • Borchardt, R. T., Cheng, C. F. and Thakker, D. R. (1975). Purification of Catechol-O-Methyltransferase by Affinity Chromatography. Biochem. Biophys. Res. Commun., 63, 69–77.

    Google Scholar 

  • Borchardt, R. T. and Thakker, D. R. (1976). Evidence for Sulfhydryl Groups at the Active Site of Catechol-O-Methyltransferase. Biochim. Biophys. Acta, 445, 498–509.

    Google Scholar 

  • Borchardt, R. T. (1977). Chemical Probes of the Active Site of Catechol-O-Methyltransferase. In Biochemistry and Function of Monoamine Enzymes, (ed., E. Usdin and N. Weiner), Marcel Dekker, New York, p. 707–720.

    Google Scholar 

  • Borchardt, R. T. (1980). N- and O-Methylation. In Enzymatic Basis of Detoxication, Vol. II, Wiley, New York, p. 43–62.

    Google Scholar 

  • Borchardt, R. T. (1981). Catechol-O-Methyltransferase: Assay, Purification and Properties. In Methods in Enzymology - Detoxication and Drug Metabolism: Conjugation and Related Systems, (ed., W. B. Jakoby), Academic Press, New York, in press.

    Google Scholar 

  • Guldberg, H. C. and Marsden, C. A. (1975). Catechol-O-Methyltransferase: Pharmacological Aspects and Physioloqical Role. Pharmacol. Rev., 27, 135–206.

    Google Scholar 

  • Lutz, W. B., Creveling, C. R., Daly, J. W. and Witkop, B. (1972). Sulfur Analogs of Dopamine and Norepinephrine. Inhibition of Catechol-O-Methyltransferase. J. Med. Chem., 15, 795–802.

    Google Scholar 

  • Nikodejevic, B., Senoh, S., Daly, J. W. and Creveling, C. R. (1970). Catechol-O-Methyltransferase. II. A New Class of Inhibitors of Catechol-O-Methyltransferase; 3,5-Dihydroxy-4-Methoxybenzoic Acid and Related Compounds. J. Pharmacol. Exptl. Therap., 174, 83–93.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Copyright information

© 1981 The Contributors

About this chapter

Cite this chapter

Borchardt, R.T., Huber, J.A. (1981). 3-Substituted-4-methoxy-5-hydroxybenzaldehydes and benzoic acids as inhibitors of catechol-O-methyltransferase. In: Usdin, E., Weiner, N., Youdim, M.B.H. (eds) Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06276-8_71

Download citation

Publish with us

Policies and ethics