Purification and characterization of an erythromycin esterase from an erythromycin-resistant Pseudomonas sp.

@article{Kim2002PurificationAC,
  title={Purification and characterization of an erythromycin esterase from an erythromycin-resistant Pseudomonas sp.},
  author={Y Kim and C G Cha and Carl Cerniglia},
  journal={FEMS microbiology letters},
  year={2002},
  volume={210 2},
  pages={239-44}
}
An erythromycin esterase (molecular mass 51200 Da) was purified from Pseudomonas sp. GD100, which was isolated from a salmon hatchery sediment sample from Washington State. The pI of the protein was 4.5-4.8. The enzyme was inhibited by 1 mM mercuric acid, and had the substrate specificity for structurally related 14-membered macrolides, which decreased in the order of oleandomycin, erythromycin A and erythromycin A enol ether. The activity for erythromycin A varied with temperature, but the… CONTINUE READING

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