Linked Life Data

6969804

Source:http://linkedlifedata.com/resource/pubmed/id/6969804

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1981-3-24
pubmed:abstractText
The resistance of some penicillins to beta-lactamase enzymes was previously attributed to the nature of their C(6) side chain. In order to find explicitly the influence of the conformation of this side chain in the enzymatic mechanism, we have analyzed by experimental and theoretical methods (X-ray diffraction, NMR, IR, PCILO) the molecular structure of six resistant penicillins and derivatives: oxacillin, cloxacillin, dicloxacillin, flucloxacillin, methicillin, nafcillin, cloxacillin sulfoxide, and oxacillinpenicilloic acid. X-ray crystallography of flucloxacillin and nafcillin is fully described. We observe that the side chains of these penicillins have no influence on the electronic properties of the penam nucleus but are much more rigid than in the sensitive ones. The molecular conformations are mostly governed by the nonbonded Van der Waals interactions and, in the oxacillins, partly by the conjugation between exocyclic groups. The lack of flexibility could result in a distorting effect on the structure of the active site of the beta-lactamase, leading to the deactivation of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1283-92
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
A multifaceted approach to the study of the side-chain conformation in beta-lactamase-resistant penicillins.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't