Structural insights into the low pH adaptation of a unique carboxylesterase from Ferroplasma: altering the pH optima of two carboxylesterases.

@article{Ohara2014StructuralII,
  title={Structural insights into the low pH adaptation of a unique carboxylesterase from Ferroplasma: altering the pH optima of two carboxylesterases.},
  author={Kazuhiro Ohara and Hideaki Unno and Yasuhiro Oshima and Miho Hosoya and Naoto Fujino and Kazutake Hirooka and Seiji Takahashi and Satoshi Yamashita and Masami Kusunoki and Toru Nakayama},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 35},
  pages={24499-510}
}
To investigate the mechanism for low pH adaptation by a carboxylesterase, structural and biochemical analyses of EstFa_R (a recombinant, slightly acidophilic carboxylesterase from Ferroplasma acidiphilum) and SshEstI (an alkaliphilic carboxylesterase from Sulfolobus shibatae DSM5389) were performed. Although a previous proteomics study by another group showed that the enzyme purified from F. acidiphilum contained an iron atom, EstFa_R did not bind to iron as analyzed by inductively coupled… CONTINUE READING
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