Linked Life Data

12903130

Source:http://linkedlifedata.com/resource/pubmed/id/12903130

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-8-7
pubmed:abstractText
Porphyrin has been reported to bind to the T psi C stem of tRNA. This site is also recognized by ribonuclease P, which is essential and ubiquitous endoribonuclease responsible for the maturation of 5' ends of tRNA precursors. Thus, we investigated the effects of porphyrins on the in vitro reaction of ribonuclease P from Escherichia coli. The results showed that some of porphyrins inhibited the reaction more strongly than any other inhibitors reported so far. In addition to the benzimidazole inhibition that we have previously reported, these unusual substrate-binding inhibitions may provide new leads for the novel anti-bacterial reagent design.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:author
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-2
pubmed:dateRevised
2006-11-30
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Porphyrins and porphines inhibit the ribonuclease P reaction in vitro.
pubmed:affiliation
Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't