Combined High-Resolution Neutron and X-ray Analysis of Inhibited Elastase Confirms the Active-Site Oxyanion Hole but Rules against a Low-Barrier Hydrogen Bond-Reference-Cited by-同舟云学术

Combined High-Resolution Neutron and X-ray Analysis of Inhibited Elastase Confirms the Active-Site Oxyanion Hole but Rules against a Low-Barrier Hydrogen Bond

Published:2009-07-15 Issue:31 Volume:131 Page:11033-11040
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Tamada Taro¹,Kinoshita Takayoshi¹,Kurihara Kazuo¹,Adachi Motoyasu¹,Ohhara Takashi¹,Imai Keisuke¹,Kuroki Ryota¹,Tada Toshiji¹

Affiliation:

1. Quantum Beam Science Directorate, Japan Atomic Energy Agency, 2-4 Shirakata-Shirane, Tokai, Ibaraki 319-1195, Japan, Department of Biological Science, Graduate School of Science, Osaka Prefecture University, 1-1 Gakuen-cho, Naka-ku, Sakai, Osaka 599-8531, Japan, and Lead Discovery Research Laboratories, Astellas Pharma, Inc., 21 Miyukigaoka, Tsukuba, Ibaraki, 305-8585, Japan

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9028846

Reference40 articles.

1. Serine Protease Mechanism and Specificity

2. Studies of the activity of chymotrypsin

3. Structure of crystalline α-chymotrypsin

4. Low-Barrier Hydrogen Bonds and Enzymic Catalysis

5. A Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Proteases

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