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Substrate uptake and protein stability relationship in mammalian histidine decarboxylase
Author(s) -
PinoÁngeles A.,
Morreale A.,
Negri A.,
SánchezJiménez F.,
MoyaGarcía A. A.
Publication year - 2010
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22587
Subject(s) - substrate (aquarium) , histidine , active site , chemistry , molecular dynamics , kinetics , protein structure , biochemistry , biophysics , enzyme , stereochemistry , biology , computational chemistry , ecology , physics , quantum mechanics
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. Proteins 2010. © 2009 Wiley‐Liss, Inc.