An Insight into the environmental effects of the pocket of the active site of the enzyme. Ab initio ONIOM molecular dynamics (MD) study on cytosine deaminase

Toshiaki Matsubara, Michel Dupuis, Misako Aida

Research output: Contribution to journalArticle

9 Citations (Scopus)


We applied the ONIOM-molecular dynamics (MD) method to cytosine deaminase to examine the environmental effects of the amino acid residues in the pocket of the active site on the substrate taking account of their thermal motion. The ab initio ONIOM-MD simulations show that the substrate uracil is strongly perturbed by the amino acid residue Ile33, which sandwiches the uracil with His62, through the steric contact due to the thermal motion. As a result, the magnitude of the thermal oscillation of the potential energy and structure of the substrate uracil significantly increases.

Original languageEnglish
Pages (from-to)458-465
Number of pages8
JournalJournal of Computational Chemistry
Issue number3
Publication statusPublished - Feb 1 2008



  • Ab initio ONIOM-molecular dynamics (MD) method
  • Active site
  • Cytosine deaminase
  • Environmental effects
  • Thermal motion

ASJC Scopus subject areas

  • Chemistry(all)
  • Computational Mathematics

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