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Common inhibition of both β-glucosidases and β-mannosidases by isofagomine lactam reflects different conformational itineraries for pyranoside hydrolysis

Lookup NU author(s): Carl Morland, Emeritus Professor Harry Gilbert

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Abstract

Glycosidase inhibition is a key process both in the pursuit of new therapeutic agents and in the drive to understand transition-state stabilisation by these remarkable enzymes. That isofagomine lactam (1) is an equally potent inhibitor of β-glucosidases and β-mannosidases (despite possessing a carbonyl group) adds to the emerging view that mannosidases and glucosidases harness distinct transition states; the β2,5 conformation for some retaining mannosidases and the 4W3 for glucosidases, both of which place O2 pseudo-equatorially.

Publication metadata

Author(s): Vincent F, Gloster TM, Macdonald J, Morland C, Stick RV, Dias FMV, Prates JAM, Fontes CMGA, Gilbert HJ, Davies GJ

Publication type: Article

Publication status: Published

Journal: ChemBioChem

Year: 2004

Volume: 5

Issue: 11

Pages: 1596-1599

ISSN (print): 1439-4227

ISSN (electronic): 1439-7633

Publisher: Wiley - VCH Verlag GmbH & Co. KGaA

URL: http://dx.doi.org/10.1002/cbic.200400169

DOI: 10.1002/cbic.200400169

PubMed id: 15515081

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Funding

Funder referenceFunder name
BBS/B/05974Biotechnology and Biological Sciences Research Council

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