Structural Dynamics of the PET-Degrading Cutinase-like Enzyme from Saccharomonospora viridis AHK190 in Substrate-Bound States Elucidates the Ca2+-Driven Catalytic Cycle.

@article{Numoto2018StructuralDO,
  title={Structural Dynamics of the PET-Degrading Cutinase-like Enzyme from Saccharomonospora viridis AHK190 in Substrate-Bound States Elucidates the Ca2+-Driven Catalytic Cycle.},
  author={N. Numoto and N. Kamiya and G. Bekker and Yuri Yamagami and S. Inaba and K. Ishii and S. Uchiyama and F. Kawai and N. Ito and M. Oda},
  journal={Biochemistry},
  year={2018},
  volume={57 36},
  pages={
          5289-5300
        }
}
  • N. Numoto, N. Kamiya, +7 authors M. Oda
  • Published 2018
  • Medicine
  • Biochemistry
  • A cutinase-type polyesterase from Saccharomonospora viridis AHK190 (Cut190) has been shown to degrade the inner block of polyethylene terephthalate. A unique feature of Cut190 is that its function and stability are regulated by Ca2+ binding. Our previous crystal structure analysis of Cut190S226P showed that one Ca2+ binds to the enzyme, which induces large conformational changes in several loop regions to stabilize an open conformation [Miyakawa, T., et al. (2015) Appl. Microbiol. Biotechnol… CONTINUE READING
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