Effect of active site mutation Phe 93 → Trp in the horse liver alcohol dehydrogenase enzyme on catalysis: A molecular dynamics study

C. Kalyanaraman, Steven D. Schwartz

Research output: Contribution to journalLetter

9 Scopus citations

Abstract

We have studied the effect of the site-directed mutation, Phe 93 → Trp, in the horse liver alcohol dehydrogenase enzyme as it relates to a specific protein motion that plays a crucial role in catalysis. Results obtained from the study suggest that the protein dynamics as it couples to reaction catalysis is not affected and in fact the coupling between the protein oscillation and the reaction coordinate is similar to that seen in the wild-type. This supports the view that this mutation distal from the NAD- cofactor does not change the way protein dynamics influences chemistry.

Original languageEnglish (US)
Pages (from-to)13111-13113
Number of pages3
JournalJournal of Physical Chemistry B
Volume106
Issue number51
DOIs
StatePublished - Dec 26 2002
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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