Computational Design of Experiment Unveils the Conformational Reaction Coordinate of GH125 α-Mannosidases-Reference-Cited by-同舟云学术

Computational Design of Experiment Unveils the Conformational Reaction Coordinate of GH125 α-Mannosidases

Published:2017-01-03 Issue:3 Volume:139 Page:1085-1088
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Alonso-Gil Santiago¹,Males Alexandra²,Fernandes Pearl Z.³,Williams Spencer J.³^ORCID,Davies Gideon J.²,Rovira Carme¹⁴^ORCID

Affiliation:

1. Departament de Química Inorgànica i Orgànica (Secció de Química Orgànica) & Institut de Química Teòrica i Computacional (IQTCUB), Universitat de Barcelona, 08028 Barcelona, Spain

2. York Structural Biology Laboratory, Department of Chemistry, The University of York, YO10 5DD York, United Kingdom

3. School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria 3010, Australia

4. Institució Catalana de Recerca i Estudis Avançats (ICREA), 08010 Barcelona, Spain

Funder

Royal Society

Ag?ncia de Gesti? d?Ajuts Universitaris i de Recerca

Australian Research Council

Secretar?a de Estado de Investigaci?n, Desarrollo e Innovaci?n

Biotechnology and Biological Sciences Research Council

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

http://pubs.acs.org/doi/pdf/10.1021/jacs.6b11247

Reference32 articles.

1. Conformational Analyses of the Reaction Coordinate of Glycosidases

2. Dissecting conformational contributions to glycosidase catalysis and inhibition

3. STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS

4. The Principle of Least Nuclear Motion and the Theory of Stereoelectronic Control

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