Construction of a new leucine dehydrogenase with preferred specificity for NADP+ by site-directed mutagenesis of the strictly NAD+-specific enzyme.

@article{Galkin1997ConstructionOA,
  title={Construction of a new leucine dehydrogenase with preferred specificity for NADP+ by site-directed mutagenesis of the strictly NAD+-specific enzyme.},
  author={A. Galkin and L. Kulakova and T. Ohshima and N. Esaki and K. Soda},
  journal={Protein engineering},
  year={1997},
  volume={10 6},
  pages={
          687-90
        }
}
On the basis of sequence comparison between NAD+-dependent leucine dehydrogenase (LeuDH) from Thermoactinomyces intermedius and NADP+-dependent dehydrogenases, a set of amino acid residues that are supposed to determine the coenzyme specificity of LeuDH were assigned. Systematic replacement of these amino acids by others was done with the aim to switch its natural coenzyme specificity to a new one preferring NADP+. Single D203A, double D203A-I204R and triple D203A-I204R-D210R mutation enzymes… Expand
Crystallization and preliminary X-ray analysis of substrate complexes of leucine dehydrogenase from Thermoactinomyces intermedius.
Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase.
...
1
2
3
...

References

SHOWING 1-10 OF 12 REFERENCES
Enzyme structure and function
Biochemistry
J. Biochem
  • J. Biochem
  • 1996
Proc. Natl Acad. Sci. USA
  • Proc. Natl Acad. Sci. USA
  • 1995
Structure
  • Structure
  • 1995
Eur. J. Biochem
  • Eur. J. Biochem
  • 1994
J. Biol. Chem
  • J. Biol. Chem
  • 1993
J. Mol. Biol
  • J. Mol. Biol
  • 1993
J. Mol. Biol
  • J. Mol. Biol
  • 1993
Eur. J. Biochem
  • Eur. J. Biochem
  • 1992
...
1
2
...