Kinetic identification of a hydrogen bonding pair in the glucoamylase-maltose transition state complex.

@article{Sierks1992KineticIO,
  title={Kinetic identification of a hydrogen bonding pair in the glucoamylase-maltose transition state complex.},
  author={Michael Sierks and Birte Svensson},
  journal={Protein engineering},
  year={1992},
  volume={5 2},
  pages={185-8}
}
Molecular recognition and site-directed mutagenesis are used in combination to identify kinetically, transition state interactions between glucoamylase (GA) and the substrate maltose. Earlier studies of mutant Glu180----Gln GA had indicated a role in substrate binding for Glu180 (Sierks, M.R., Ford, C., Reilly, P.J. and Svensson, B. (1990) Protein Engng, 3, 193-198). Here, changes in activation energies calculated from measured kcat/Km values for a series of deoxygenated maltose analogues… CONTINUE READING

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