Substrate uptake and protein stability relationship in mammalian histidine decarboxylase

Proteins. 2010 Jan;78(1):154-61. doi: 10.1002/prot.22587.


There is some evidence linking the substrate entrance in the active site of mammalian histidine decarboxylase and an increased stability against proteolytic degradation. In this work, we study the basis of this relationship by means of protein structure network analysis and molecular dynamics simulations. We find that the substrate binding to the active site influences the conformation of a flexible region sensible to proteolytic degradation and observe how formation of the Michaelis-Menten complex increases stability in the conformation of this region.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Histidine Decarboxylase / chemistry*
  • Histidine Decarboxylase / metabolism*
  • Mammals / metabolism
  • Molecular Dynamics Simulation
  • Motion
  • Protein Binding
  • Protein Conformation
  • Protein Multimerization
  • Protein Stability
  • Substrate Specificity


  • Histidine Decarboxylase