Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism.

@article{Xu2008NovelIF,
  title={Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism.},
  author={Yue Xu and Yoshitaka Nakajima and Kiyoshi Ito and Heng Zheng and Hiroshi Oyama and Ulrich Heiser and Torsten M Hoffmann and Ulf-Torsten G{\"a}rtner and Hans-Ulrich Demuth and Tadashi Yoshimoto},
  journal={Journal of molecular biology},
  year={2008},
  volume={375 3},
  pages={
          708-19
        }
}
A new inhibitor, H-Ala-Ile-pyrrolidin-2-yl boronic acid, was developed as an inhibitor against prolyl tripeptidyl aminopeptidase with a K(i) value of 88.1 nM. The structure of the prolyl tripeptidyl aminopeptidase complexed with the inhibitor (enzyme-inhibitor complex) was determined at 2.2 A resolution. The inhibitor was bound to the active site through a covalent bond between Ser603 and the boron atom of the inhibitor. This structure should closely mimic the structure of the reaction… CONTINUE READING
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