Linked Life Data

21651455

Source:http://linkedlifedata.com/resource/pubmed/id/21651455

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2011-6-17
pubmed:abstractText
INTRODUCTION: Bacterial enoyl acyl carrier protein reductase (ENR) specificity reduces the double bond in enoyl thioester substrates in the final enzymatic step of the elongation cycle of the fatty acid synthase-II pathway. Its function is essential for bacterial organism survival, making it an attractive target for the development of novel antibiotics. The structural features and therapeutic potential of this enzyme have stimulated the rational design of ENR inhibitors, and important progress has been achieved to date. AREAS COVERED: This review describes recent advances made in the search for ENR inhibitors, as reflected by patent applications filed from 2006 to 2010, together with an overview of the relevant literature. The first section of this paper provides a background of the biology of ENR, followed by a description of its structure and function. The main section describes the substrate specificities for ENR, and the structure-based rational design of patent inhibitors originating from different companies and academic groups. EXPERT OPINION: The increase in the number of ENR inhibitors bodes well for the development of new therapeutics against multidrug-resistant bacteria. The challenge is now to improve the pharmacokinetic parameters of these inhibitors and translate them into clinical studies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1744-7674
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1007-22
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Enoyl acyl carrier protein reductase inhibitors: a patent review (2006 - 2010).
pubmed:affiliation
Guangzhou Institutes of Biomedicine and Health, Key Laboratory of Regenerative Biology and Institute of Chemical Biology, Chinese Academy of Sciences, No. 190, Kaiyuan Avenue, Science Park, Guangzhou, 510530, China.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't