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Article: Mapping the active site of the bacterial enzyme LpxC using novel carbohydrate-based hydroxamic acid inhibitors

TitleMapping the active site of the bacterial enzyme LpxC using novel carbohydrate-based hydroxamic acid inhibitors
Authors
KeywordsCarbohydrate Analog
Deacetylase
Enzyme Inhibitor
Hydroxamic Acid
Issue Date2005
PublisherTaylor & Francis Inc. The Journal's web site is located at http://www.tandf.co.uk/journals/titles/07328303.asp
Citation
Journal Of Carbohydrate Chemistry, 2005, v. 24 n. 4-6, p. 583-609 How to Cite?
AbstractLpxC (UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase), an enzyme involved in the biosynthesis of lipid A, is crucial for the growth of Gram-negative bacteria. This enzyme has accordingly been identified as a potential target for the development of novel antibiotics against Gram-negative bacteria. The carbohydrate-derived hydroxamic acid 1 (1,5-anhydro-2-C- (carboxymethyl N-hydroxyamide)-2-deoxy-3-O-myristoyl-D-glucitol) was previously shown to exhibit a wide spectrum of inhibitory activity against LpxC enzymes. Here we describe the preparation of seven analogs of 1 and their enzymatic evaluation. Two of the hydroxyl groups (OH-3 and 6) of the GlcNAc residue were found to be involved in the binding interaction, and there is an important hydrophobic interaction in the vicinity O-3 position with the enzyme that recognizes aromatic as well as aliphatic substituents. Copyright © Taylor & Francis, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/167970
ISSN
2015 Impact Factor: 0.738
2015 SCImago Journal Rankings: 0.496
References

 

DC FieldValueLanguage
dc.contributor.authorLi, Xen_US
dc.contributor.authorMcclerren, ALen_US
dc.contributor.authorRaetz, CRHen_US
dc.contributor.authorHindsgaul, Oen_US
dc.date.accessioned2012-10-08T03:13:33Z-
dc.date.available2012-10-08T03:13:33Z-
dc.date.issued2005en_US
dc.identifier.citationJournal Of Carbohydrate Chemistry, 2005, v. 24 n. 4-6, p. 583-609en_US
dc.identifier.issn0732-8303en_US
dc.identifier.urihttp://hdl.handle.net/10722/167970-
dc.description.abstractLpxC (UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase), an enzyme involved in the biosynthesis of lipid A, is crucial for the growth of Gram-negative bacteria. This enzyme has accordingly been identified as a potential target for the development of novel antibiotics against Gram-negative bacteria. The carbohydrate-derived hydroxamic acid 1 (1,5-anhydro-2-C- (carboxymethyl N-hydroxyamide)-2-deoxy-3-O-myristoyl-D-glucitol) was previously shown to exhibit a wide spectrum of inhibitory activity against LpxC enzymes. Here we describe the preparation of seven analogs of 1 and their enzymatic evaluation. Two of the hydroxyl groups (OH-3 and 6) of the GlcNAc residue were found to be involved in the binding interaction, and there is an important hydrophobic interaction in the vicinity O-3 position with the enzyme that recognizes aromatic as well as aliphatic substituents. Copyright © Taylor & Francis, Inc.en_US
dc.languageengen_US
dc.publisherTaylor & Francis Inc. The Journal's web site is located at http://www.tandf.co.uk/journals/titles/07328303.aspen_US
dc.relation.ispartofJournal of Carbohydrate Chemistryen_US
dc.subjectCarbohydrate Analogen_US
dc.subjectDeacetylaseen_US
dc.subjectEnzyme Inhibitoren_US
dc.subjectHydroxamic Aciden_US
dc.titleMapping the active site of the bacterial enzyme LpxC using novel carbohydrate-based hydroxamic acid inhibitorsen_US
dc.typeArticleen_US
dc.identifier.emailLi, X:xuechenl@hku.hken_US
dc.identifier.authorityLi, X=rp00742en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1081/CAR-200068781en_US
dc.identifier.scopuseid_2-s2.0-27844561171en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-27844561171&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume24en_US
dc.identifier.issue4-6en_US
dc.identifier.spage583en_US
dc.identifier.epage609en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLi, X=24168958800en_US
dc.identifier.scopusauthoridMcClerren, AL=7801327115en_US
dc.identifier.scopusauthoridRaetz, CRH=7102514726en_US
dc.identifier.scopusauthoridHindsgaul, O=7102966220en_US

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