Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone.

@article{VaajeKolstad2004InteractionsOA,
  title={Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone.},
  author={Gustav Vaaje-Kolstad and Andrea Vasella and Martin G. Peter and Catharina Netter and Douglas R. Houston and Bj{\o}rge Westereng and Bj{\o}rnar Synstad and Vincent G H Eijsink and Daan M F van Aalten},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 5},
  pages={
          3612-9
        }
}
We describe enzymological and structural analyses of the interaction between the family 18 chitinase ChiB from Serratia marcescens and the designed inhibitor N,N'-diacetylchitobionoxime-N-phenylcarbamate (HM508). HM508 acts as a competitive inhibitor of this enzyme with a K(i) in the 50 microM range. Active site mutants of ChiB show K(i) values ranging from 1 to 200 microM, providing insight into some of the interactions that determine inhibitor affinity. Interestingly, the wild type enzyme… CONTINUE READING

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