Journal article

Mannosidase mechanism: at the intersection of conformation and catalysis

Carme Rovira, Alexandra Males, Gideon J Davies, Spencer J Williams

CURRENT OPINION IN STRUCTURAL BIOLOGY | CURRENT BIOLOGY LTD | Published : 2020

Abstract

Mannosidases are a diverse group of enzymes that are important in the biological processing of mannose-containing polysaccharides and complex glycoconjugates. They are found in 12 of the >160 sequence-based glycosidase families. We discuss evidence that nature has evolved a small set of common mechanisms that unite almost all of these mannosidase families. Broadly, mannosidases (and the closely related rhamnosidases) perform catalysis through just two conformations of the oxocarbenium ion-like transition state: a B2,5 (or enantiomeric 2,5B) boat and a 3H4 half-chair. This extends to a new family (GT108) of GDPMan-dependent β-1,2-mannosyltransferases/phosphorylases that perform mannosyl trans..

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University of Melbourne Researchers

Grants

Awarded by Australian Research Council (ARC)


Awarded by Spanish Ministry of Science, Innovation and Universities (MICINN)


Awarded by Agency for Management of University and Research Grants (AGAUR)


Funding Acknowledgements

The Australian Research Council (ARC, DP180101957), the Spanish Ministry of Science, Innovation and Universities (MICINN, grants CTQ2017-85496-P and MDM-2017-0767) and the Agency for Management of University and Research Grants (AGAUR, grant 2017SGR-1189) are thanked for financial support. GJD is supported by the Royal Society through the Ken Murray Research Professorship. We thank Alba Nin-Hill for technical assistance with one of the figures of the manuscript.