Inhibition of a bacterial O-GlcNAcase homologue by lactone and lactam derivatives: structural, kinetic and thermodynamic analyses View Full Text


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Article Info

DATE

2010-08-06

AUTHORS

Yuan He, Abigail K. Bubb, Keith A. Stubbs, Tracey M. Gloster, Gideon J. Davies

ABSTRACT

The dynamic, intracellular, O-GlcNAc modification is of continuing interest and one whose study through targeted “chemical genetics” approaches is set to increase. Of particular importance is the inhibition of the O-GlcNAc hydrolase, O-GlcNAcase (OGA), since this provides a route to elevate cellular O-GlcNAc levels, and subsequent phenotypic evaluation. Such a small molecule approach complements other methods and potentially avoids changes in protein–protein interactions that manifest themselves in molecular biological approaches to O-GlcNAc transferase knockout or over-expression. Here we describe the kinetic, thermodynamic and three-dimensional structural analysis of a bacterial OGA analogue from Bacteroides thetaiotaomicron, BtGH84, in complex with a lactone oxime (LOGNAc) and a lactam form of N-acetylglucosamine and compare their binding signatures with that of the more potent inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino N-phenyl carbamate (PUGNAc). We show that both LOGNAc and the N-acetyl gluconolactam are significantly poorer inhibitors than PUGNAc, which may reflect poorer mimicry of transition state geometry and steric clashes with the enzyme upon binding; drawbacks that the phenyl carbamate adornment of PUGNAc helps mitigate. Implications for the design of future generations of inhibitors are discussed. More... »

PAGES

829-839

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00726-010-0700-6

DOI

http://dx.doi.org/10.1007/s00726-010-0700-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1003664937

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/20689974


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