Structural basis for an exceptionally strong preference for asparagine residue at the S2 subsite of Stenotrophomonas maltophilia dipeptidyl peptidase 7

Structural basis for an exceptionally strong preference for asparagine residue at the S2 subsite of Stenotrophomonas maltophilia dipeptidyl peptidase 7

Abstract The emergence of drug-resistant bacteria has become a major problem worldwide. Bacterial dipeptidyl peptidases 7 and 11 (DPP7s and DPP11s), belonging to the family-S46 peptidases, are important enzymes for bacterial growth and are not present in mammals. Therefore, specific inhibitors for t...

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Main Authors: Akihiro Nakamura, Yoshiyuki Suzuki, Yasumitsu Sakamoto, Saori Roppongi, Chisato Kushibiki, Natsuri Yonezawa, Masato Takahashi, Yosuke Shida, Hiroaki Gouda, Takamasa Nonaka, Nobutada Tanaka, Wataru Ogasawara
Format: article
Language:EN
Published: Nature Portfolio 2021
Subjects:
Medicine
R
Science
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Online Access:https://doaj.org/article/b6c00e65e97349549b97e2a4e38cc085
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https://doaj.org/article/b6c00e65e97349549b97e2a4e38cc085

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