Structural features of mammalian histidine decarboxylase reveal the basis for specific inhibition

Br J Pharmacol. 2009 May;157(1):4-13. doi: 10.1111/j.1476-5381.2009.00219.x.

Abstract

For a long time the structural and molecular features of mammalian histidine decarboxylase (EC 4.1.1.22), the enzyme that produces histamine, have evaded characterization. We overcome the experimental problems for the study of this enzyme by using a computer-based modelling and simulation approach, and have now the conditions to use histidine decarboxylase as a target in histamine pharmacology. In this review, we present the recent (last 5 years) advances in the structure-function relationship of histidine decarboxylase and the strategy for the discovery of new drugs.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Computer Simulation*
  • Drug Design
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology
  • Histidine Decarboxylase / antagonists & inhibitors
  • Histidine Decarboxylase / chemistry*
  • Histidine Decarboxylase / physiology
  • Ligands
  • Models, Molecular*
  • Molecular Structure
  • Structure-Activity Relationship
  • Thermodynamics

Substances

  • Enzyme Inhibitors
  • Ligands
  • Histidine Decarboxylase