The Crystal Structure of Peptidase Toward Drug Discovery

DOI:10.15011//jasma.36.360106
Int. J. Microgravity Sci. Appl. 2019p360106
Author
Y. SAKAMOTO, S. ROPPONGI, Y. SUZUKI, T. ISHIHARA, K. HIDAKA, A. NAKAMURA, N. HONMA, W. OGASAWARA and N. TANAKA
Organization
School of Pharmacy, Iwate Medical University, Dept. of Bioengineering, Nagaoka University of Technology, Biomedical Research Institute, Advanced Industrial Science and Technology, The Faculty of Pharmaceutical Sciences, School of Pharmacy, Showa University, Center for Molecular Analysis, Showa University
Abstract
Dipeptidyl amino peptidase is well known as a drug target of diabetes. Therefore, the existence of many types of DPPs in many organisms has been often overlooked by clinical researchers. Human DPP4 is involved in the inactivation of incretin for the control of blood glucose levels. Meanwhile, some bacterial DPPs are involved in energy metabolism in Non-Fermenting Gram-Negative Rods (NFGNRs). NFGNRs utilize peptides or proteins as energy and carbon sources instead of carbohydrates. Bacterial DPPs are composed of two families (Clan SC S9, Clan PA S46). Clan SC S9 family DPPs are also seen in animals. By contrast, Clan PA S46 family DPPs are only found in bacteria. Additionally, substrate specificity of Clan PA S46 DPPs are completely different from Clan SC S9 DPPs. Considering these features together, bacterial DPPs may be potential target molecules for antimicrobials.
Keyword(s)
DPP, NFGNR, Antibiotics, Crystallization, PCG.
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Received 13 December 2018, Accepted 25 January 2019, Published 31 January 2019.

© The Japan Society of Microgravity Applicaiton

この投稿文は次の言語で読めます: Japanese

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