Substrate uptake and protein stability relationship in mammalian histidine decarboxylase.
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.
Pino-Angeles
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A
Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Universidad de Málaga, Campus de Teatinos, Málaga, Spain.
Morreale
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A
Negri
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A
Sánchez-Jiménez
F
F
Moya-García
A A
AA
D000818:Animals; D006640:Histidine Decarboxylase / Q000737:chemistry* / Q000378:metabolism*; D008322:Mammals / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D009038:Motion; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization; D055550:Protein Stability; D013379:Substrate Specificity
D006640:Histidine Decarboxylase