Unlocking the Hydrolytic Mechanism of GH92 α‐1,2‐Mannosidases: Computation Inspires the use of C‐Glycosides as Michaelis Complex Mimics

Author:

Alonso‐Gil Santiago1ORCID,Parkan Kamil2ORCID,Kaminský Jakub3ORCID,Pohl Radek3ORCID,Miyazaki Takatsugu4ORCID

Affiliation:

1. Department of Structural and Computational Biology Max F. Perutz Laboratories University of Vienna Dr.-Bohr-Gasse 9 1030 Vienna Austria

2. Department of Chemistry of Natural Compounds University of Chemistry and Technology Technická 5 166 28 Prague Czech Republic

3. Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences Gilead Sciences & IOCB Research Centre Czech Academy of Sciences Flemingovo nám. 2 166 10 Prague Czech Republic

4. Research Institute of Green Science and Technology Shizuoka University 836 Ohya, Suruga-ku Shizuoka 422-8529 Japan

Funder

H2020 Marie Skłodowska-Curie Actions

Gilead Sciences

Publisher

Wiley

Subject

General Chemistry,Catalysis,Organic Chemistry

Reference28 articles.

1. N-glycan processing in ER quality control

2. Glycoprotein folding, quality control and ER-associated degradation

3. H. H. Freeze H. Schachter. Genetic Disorders of Glycosylation. In: A. Varki R. D. Cummings J. D. Esko editors.Essentials of Glycobiology. 2nd edition Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press 2009. Chapter 42.

4. The carbohydrate-active enzymes database (CAZy) in 2013

5. The molecular characterization of a novel GH38 α-mannosidase from the crenarchaeon Sulfolobus solfataricus revealed its ability in de-mannosylating glycoproteins

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