Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues-Reference-Cited by-同舟云学术

Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues

Published:2018-02-09 Issue:1 Volume:8 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Roppongi Saori,Suzuki Yoshiyuki,Tateoka Chika,Fujimoto Mayu,Morisawa Saori,Iizuka Ippei,Nakamura Akihiro,Honma Nobuyuki,Shida Yosuke,Ogasawara Wataru,Tanaka Nobutada^ORCID,Sakamoto Yasumitsu^ORCID,Nonaka Takamasa

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41598-018-21056-y.pdf

Reference75 articles.

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3. Yoshimoto, T. & Tsuru, D. Proline-specific dipeptidyl aminopeptidase from Flavobacterium meningosepticum. J. Biochem. 91, 1899–1906 (1982).

4. Cox, S. W. & Eley, B. M. Detection of cathepsin B- and L-, elastase-, tryptase-, trypsin-, and dipeptidyl peptidase IV-like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin. J. Periodontal Res. 24, 353–361 (1989).

5. Mayo, B. et al. Molecular cloning and sequence analysis of the X-prolyl dipeptidyl aminopeptidase gene from Lactococcus lactis subsp. cremoris. Appl. Environ. Microbiol. 57, 38–44 (1991).

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