Generic placeholder image

Current Enzyme Inhibition

Editor-in-Chief

ISSN (Print): 1573-4080
ISSN (Online): 1875-6662

Dopamine β-Monooxygenase: Mechanism, Substrates and Inhibitors

Author(s): Alexandre Beliaev, Humberto Ferreira, David A. Learmonth and Patricio Soares-da-Silva

Volume 5, Issue 1, 2009

Page: [27 - 43] Pages: 17

DOI: 10.2174/157340809787314265

Price: $65

Abstract

Dopamine β-monooxygenase (DBM) catalyses the conversion of dopamine to norepinephrine in the catecholamine biosynthetic pathway. The substrate specificity of DBM is wide and the enzyme is capable of performing a variety of oxidations. While the crystal structure of DBM is not yet available, various indirect data allow insight into the enzymes machinery. Considered an attractive therapeutic target for the treatment of hypertension and congestive heart failure, DBM and its inhibitors have received attention by medicinal chemists over the last four decades. Although several QSAR models for DBM inhibitors have been generated, these models are actually unable to explain the exceptionally high potency of the latest generation of inhibitors.

Keywords: Dopamine β-monooxygenase, dopamine β-hydroxylase, inhibitor, imidazolethione, nepicastat, BIA 5-453, CHF


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy