File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1081/CAR-200068781
- Scopus: eid_2-s2.0-27844561171
- WOS: WOS:000231388300017
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Mapping the active site of the bacterial enzyme LpxC using novel carbohydrate-based hydroxamic acid inhibitors
Title | Mapping the active site of the bacterial enzyme LpxC using novel carbohydrate-based hydroxamic acid inhibitors |
---|---|
Authors | |
Keywords | Carbohydrate Analog Deacetylase Enzyme Inhibitor Hydroxamic Acid |
Issue Date | 2005 |
Publisher | Taylor & 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? |
Abstract | LpxC (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 Identifier | http://hdl.handle.net/10722/167970 |
ISSN | 2023 Impact Factor: 1.2 2023 SCImago Journal Rankings: 0.268 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Li, X | en_US |
dc.contributor.author | Mcclerren, AL | en_US |
dc.contributor.author | Raetz, CRH | en_US |
dc.contributor.author | Hindsgaul, O | en_US |
dc.date.accessioned | 2012-10-08T03:13:33Z | - |
dc.date.available | 2012-10-08T03:13:33Z | - |
dc.date.issued | 2005 | en_US |
dc.identifier.citation | Journal Of Carbohydrate Chemistry, 2005, v. 24 n. 4-6, p. 583-609 | en_US |
dc.identifier.issn | 0732-8303 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/167970 | - |
dc.description.abstract | LpxC (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.language | eng | en_US |
dc.publisher | Taylor & Francis Inc. The Journal's web site is located at http://www.tandf.co.uk/journals/titles/07328303.asp | en_US |
dc.relation.ispartof | Journal of Carbohydrate Chemistry | en_US |
dc.subject | Carbohydrate Analog | en_US |
dc.subject | Deacetylase | en_US |
dc.subject | Enzyme Inhibitor | en_US |
dc.subject | Hydroxamic Acid | en_US |
dc.title | Mapping the active site of the bacterial enzyme LpxC using novel carbohydrate-based hydroxamic acid inhibitors | en_US |
dc.type | Article | en_US |
dc.identifier.email | Li, X:xuechenl@hku.hk | en_US |
dc.identifier.authority | Li, X=rp00742 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1081/CAR-200068781 | en_US |
dc.identifier.scopus | eid_2-s2.0-27844561171 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-27844561171&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 24 | en_US |
dc.identifier.issue | 4-6 | en_US |
dc.identifier.spage | 583 | en_US |
dc.identifier.epage | 609 | en_US |
dc.identifier.isi | WOS:000231388300017 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Li, X=24168958800 | en_US |
dc.identifier.scopusauthorid | McClerren, AL=7801327115 | en_US |
dc.identifier.scopusauthorid | Raetz, CRH=7102514726 | en_US |
dc.identifier.scopusauthorid | Hindsgaul, O=7102966220 | en_US |
dc.identifier.issnl | 0732-8303 | - |