The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

Chem Commun (Camb). 2010 Dec 21;46(47):8974-6. doi: 10.1039/c0cc02988b. Epub 2010 Oct 25.

Abstract

Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Alanine / chemistry*
  • Amino Acid Substitution
  • Catalysis
  • Catalytic Domain
  • Escherichia coli / enzymology
  • Isoleucine / chemistry*
  • Kinetics
  • Molecular Dynamics Simulation
  • Mutation
  • NADP / chemistry
  • NADP / metabolism
  • Tetrahydrofolate Dehydrogenase / genetics
  • Tetrahydrofolate Dehydrogenase / metabolism*

Substances

  • Isoleucine
  • NADP
  • Tetrahydrofolate Dehydrogenase
  • Alanine