Linked Life Data

16323831

Source:http://linkedlifedata.com/resource/pubmed/id/16323831

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
2005-12-5
pubmed:abstractText
[structure: see text] Molecular clips functionalized by phosphonate or phosphate groups bind thiamine diphosphate (TPP) and S-adenosylmethionine (SAM) with high affinity in water; both sulfur-based cofactors transfer organic groups to biomolecules. For TPP, various analytical tools point toward a simultaneous insertion of both heterocyclic rings into the electron-rich clip cavity. Similarly, SAM is also embedded with its sulfonium moiety inside the receptor cavity. This paves the way for enzyme models and direct interference with enzymatic processes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-3263
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10227-37
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Inclusion of thiamine diphosphate and S-adenosylmethionine at their chemically active sites.
pubmed:affiliation
Department of Chemistry, University of Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany. schradet@staff.uni-marburg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't