“Newton’s cradle” proton relay with amide–imidic acid tautomerization in inverting cellulase visualized by neutron crystallography-Reference-Cited by-同舟云学术

“Newton’s cradle” proton relay with amide–imidic acid tautomerization in inverting cellulase visualized by neutron crystallography

Published:2015-08-07 Issue:7 Volume:1 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Nakamura Akihiko¹,Ishida Takuya¹,Kusaka Katsuhiro²^ORCID,Yamada Taro²,Fushinobu Shinya³,Tanaka Ichiro²,Kaneko Satoshi⁴,Ohta Kazunori⁵,Tanaka Hiroaki⁶^ORCID,Inaka Koji⁷,Higuchi Yoshiki⁸,Niimura Nobuo²,Samejima Masahiro¹,Igarashi Kiyohiko¹

Affiliation:

1. Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.

2. Frontier Research Center for Applied Atomic Sciences, Ibaraki University, Ibaraki 319-1106, Japan.

3. Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.

4. Department of Subtropical Biochemistry and Biotechnology, Faculty of Agriculture, University of the Ryukyus, Okinawa 903-0213, Japan.

5. Japanese Experiment Module (JEM) Utilization Center, Japan Aerospace Exploration Agency, Ibaraki 305-8505, Japan.

6. Confocal Science Inc., Tokyo 101-0032, Japan.

7. Maruwa Foods and Biosciences Inc., Nara 639-1123, Japan.

8. Department of Life Science, University of Hyogo, Hyogo 678-1297, Japan.

Abstract

A study of the visualization of proton relay in cellulase by neutron crystallography.

Funder

Japan Aerospace Exploration Agency

Ministry of Education, Culture, Sports, Science, and Technology

Japan Society for the Promotion of Science

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference32 articles.

1. Mechanisms of enzymatic glycoside hydrolysis;McCarter J. D.;Curr. Opin. Struct. Biol.,1994

2. The carbohydrate-active enzymes database (CAZy) in 2013;Lombard V.;Nucleic Acids Res.,2013

3. Structures of mutants of cellulase Cel48F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action;Parsiegla G.;J. Mol. Biol.,2008

4. The active site of cellobiohydrolase Cel6A from Trichoderma reesei: The roles of aspartic acids D221 and D175;Koivula A.;J. Am. Chem. Soc.,2002

5. Streptococcus pneumoniae endohexosaminidase D, structural and mechanistic insight into substrate-assisted catalysis in family 85 glycoside hydrolases;Abbott D. W.;J. Biol. Chem.,2009

Cited by 84 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. SIRT5 mutants reveal the role of conserved asparagine and glutamine residues in the NAD⁺‐binding pocket;FEBS Letters;2024-06-20

2. 1H, 13C and 15N backbone resonance assignment of Cel45A from Phanerochaete chrysosporium;Biomolecular NMR Assignments;2024-06-18

3. Charge neutralization and β-elimination cleavage mechanism of family 42 L-rhamnose-α-1,4-D-glucuronate lyase revealed using neutron crystallography;Journal of Biological Chemistry;2024-03

4. The first crystal structure of a family 45 glycoside hydrolase from a brown‐rot fungus, Gloeophyllum trabeumGtCel45A;FEBS Open Bio;2024-02-04

5. Overlooked Hydrogen Bond in a Blue Copper Protein Uncovered by Neutron and Sub-Ångström Resolution X-ray Crystallography;Biochemistry;2024-01-17