Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-03-26

AUTHORS

Rebecca J Dennis, Edward J Taylor, Matthew S Macauley, Keith A Stubbs, Johan P Turkenburg, Samuel J Hart, Gary N Black, David J Vocadlo, Gideon J Davies

ABSTRACT

O-GlcNAc is an abundant post-translational modification of serine and threonine residues of nucleocytoplasmic proteins. This modification, found only within higher eukaryotes, is a dynamic modification that is often reciprocal to phosphorylation. In a manner analogous to phosphatases, a glycoside hydrolase termed O-GlcNAcase cleaves O-GlcNAc from modified proteins. Enzymes with high sequence similarity to human O-GlcNAcase are also found in human pathogens and symbionts. We report the three-dimensional structure of O-GlcNAcase from the human gut symbiont Bacteroides thetaiotaomicron both in its native form and in complex with a mimic of the reaction intermediate. Mutagenesis and kinetics studies show that the bacterial enzyme, very similarly to its human counterpart, operates via an unusual 'substrate-assisted' catalytic mechanism, which will inform the rational design of enzyme inhibitors. More... »

PAGES

365-371

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb1079

DOI

http://dx.doi.org/10.1038/nsmb1079

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022184102

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16565725


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