Free energy requirement for domain movement of an enzyme

J Biol Chem. 2000 Jun 23;275(25):18939-45. doi: 10.1074/jbc.275.25.18939.


Domain movement is sometimes essential for substrate recognition by an enzyme. X-ray crystallography of aminotransferase with a series of aliphatic substrates showed that the domain movement of aspartate aminotransferase was changed dramatically from an open to a closed form by the addition of only one CH(2) to the side chain of the C4 substrate CH(3)(CH(2))C((alpha))H(NH(3)(+))COO(-). These crystallographic results and reaction kinetics (Kawaguchi, S., Nobe, Y., Yasuoka, J., Wakamiya, T., Kusumoto, S., and Kuramitsu, S. (1997) J. Biochem. (Tokyo) 122, 55-63; Kawaguchi, S. and Kuramitsu, S. (1998) J. Biol. Chem. 273, 18353-18364) enabled us to estimate the free energy required for the domain movement.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspartate Aminotransferases / chemistry
  • Aspartate Aminotransferases / metabolism*
  • Base Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • DNA Primers
  • Kinetics
  • Models, Molecular
  • Protein Conformation


  • DNA Primers
  • Aspartate Aminotransferases

Associated data

  • PDB/1C9C
  • PDB/1CQ6
  • PDB/1CQ7
  • PDB/1CQ8