The periplasmic cyclodextrin binding protein CymE from Klebsiella oxytoca and its role in maltodextrin and cyclodextrin transport.

@article{Pajatsch1998ThePC,
  title={The periplasmic cyclodextrin binding protein CymE from Klebsiella oxytoca and its role in maltodextrin and cyclodextrin transport.},
  author={M. Pajatsch and M. Gerhart and R. Peist and R. Horlacher and W. Boos and A. B{\"o}ck},
  journal={Journal of bacteriology},
  year={1998},
  volume={180 10},
  pages={
          2630-5
        }
}
Klebsiella oxytoca M5a1 has the capacity to transport and to metabolize alpha-, beta- and gamma-cyclodextrins. Cyclodextrin transport is mediated by the products of the cymE, cymF, cymG, cymD, and cymA genes, which are functionally homologous to the malE, malF, malG, malK, and lamB gene products of Escherichia coli. CymE, which is the periplasmic binding protein, has been overproduced and purified. By substrate-induced fluorescence quenching, the binding of ligands was analyzed. CymE bound… Expand
CymA of Klebsiella oxytoca outer membrane: binding of cyclodextrins and study of the current noise of the open channel.
A novel intracellular dextranase derived from Paenibacillus sp. 598K with an ability to degrade cycloisomaltooligosaccharides
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 49 REFERENCES
Genetics of a novel starch utilisation pathway present in Klebsiella oxytoca.
Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins.
The recognition of maltodextrins by Escherichia coli.
  • T. Ferenci
  • Biology, Medicine
  • European journal of biochemistry
  • 1980
Enzymology of the Cyclodextrins
Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein.
...
1
2
3
4
5
...