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2vr4

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[[Image:2vr4.jpg|left|200px]]
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{{STRUCTURE_2vr4| PDB=2vr4 | SCENE= }}
{{STRUCTURE_2vr4| PDB=2vr4 | SCENE= }}
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'''TRANSITION-STATE MIMICRY IN MANNOSIDE HYDROLYSIS: CHARACTERISATION OF TWENTY SIX INHIBITORS AND INSIGHT INTO BINDING FROM LINEAR FREE ENERGY RELATIONSHIPS AND 3-D STRUCTURE'''
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===TRANSITION-STATE MIMICRY IN MANNOSIDE HYDROLYSIS: CHARACTERISATION OF TWENTY SIX INHIBITORS AND INSIGHT INTO BINDING FROM LINEAR FREE ENERGY RELATIONSHIPS AND 3-D STRUCTURE===
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==Overview==
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Enzyme inhibition through mimicry of the transition state is a major area for the design of new therapeutic agents. Emerging evidence suggests that many retaining glycosidases that are active on alpha- or beta-mannosides harness unusual B2,5 (boat) transition states. Here we present the analysis of 25 putative beta-mannosidase inhibitors, whose Ki values range from nanomolar to millimolar, on the Bacteroides thetaiotaomicron beta-mannosidase BtMan2A. B2,5 or closely related conformations were observed for all tightly binding compounds. Subsequent linear free energy relationships that correlate log Ki with log Km/kcat for a series of active center variants highlight aryl-substituted mannoimidazoles as powerful transition state mimics in which the binding energy of the aryl group enhances both binding and the degree of transition state mimicry. Support for a B2,5 transition state during enzymatic beta-mannosidase hydrolysis should also facilitate the design and exploitation of transition state mimics for the inhibition of retaining alpha-mannosidases--an area that is emerging for anticancer therapeutics.
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(as it appears on PubMed at http://www.pubmed.gov), where 18408714 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18408714}}
==About this Structure==
==About this Structure==
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[[Category: Mannosidase]]
[[Category: Mannosidase]]
[[Category: Transition state mimic]]
[[Category: Transition state mimic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:31:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:17:00 2008''

Revision as of 14:17, 27 July 2008

Image:2vr4.png

Template:STRUCTURE 2vr4

TRANSITION-STATE MIMICRY IN MANNOSIDE HYDROLYSIS: CHARACTERISATION OF TWENTY SIX INHIBITORS AND INSIGHT INTO BINDING FROM LINEAR FREE ENERGY RELATIONSHIPS AND 3-D STRUCTURE

Template:ABSTRACT PUBMED 18408714

About this Structure

2VR4 is a Single protein structure of sequence from Bacteroides thetaiotaomicron. Full crystallographic information is available from OCA.

Reference

Structural and biochemical evidence for a boat-like transition state in beta-mannosidases., Tailford LE, Offen WA, Smith NL, Dumon C, Morland C, Gratien J, Heck MP, Stick RV, Bleriot Y, Vasella A, Gilbert HJ, Davies GJ, Nat Chem Biol. 2008 May;4(5):306-12. PMID:18408714

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