Promiscuity of Carbonic Anhydrase II. Unexpected Ester Hydrolysis of Carbohydrate-Based Sulfamate Inhibitors-Reference-Cited by-同舟云学术

Promiscuity of Carbonic Anhydrase II. Unexpected Ester Hydrolysis of Carbohydrate-Based Sulfamate Inhibitors

Published:2011-10-19 Issue:45 Volume:133 Page:18452-18462
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lopez Marie¹,Vu Hoan¹,Wang Conan K.¹,Wolf Maarten G.²,Groenhof Gerrit²,Innocenti Alessio³,Supuran Claudiu T.³,Poulsen Sally-Ann¹

Affiliation:

1. Eskitis Institute for Cell and Molecular Therapies, Griffith University, Nathan, Queensland 4111, Australia

2. Biomolecular Chemistry Group, Theoretical and Computational Biophysics Department, Max Planck Institute of Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany

3. Polo Scientifico, Laboratorio di Chimica Bioinorganica, Università degli Studi di Firenze, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja207855c

Reference46 articles.

1. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators

2. Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding

3. What makes an enzyme promiscuous?

4. Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II.

5. The 'evolvability' of promiscuous protein functions

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