Linked Life Data

7693511

Source:http://linkedlifedata.com/resource/pubmed/id/7693511

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-12-3
pubmed:abstractText
There is a considerable degree of ambiguity in the literature regarding the role of the 2',3'-cyclic phosphodiesters formed during the reaction of RNA cleavage catalysed by ribonuclease. Usually the reaction is considered to take place in two steps: in the first step there is a transphosphorylation of the RNA 3',5'-phosphodiester bond broken yielding a 2',3'-cyclic phosphodiester which in the second step is hydrolysed to a 3'-nucleotide. Although in many occasions, either explicitly or implicitly, the reaction is treated as taking place sequentially, this is not the case as it has been shown that the 2',3'-phosphodiesters are actually released to the medium as true products of the reaction and that no hydrolysis of these cyclic compounds takes place until all the susceptible 3',5'-phosphodiester bonds have been cyclised. Comparison of the hydrolysis and alcoholysis of the 2',3'-phosphodiesters catalysed by RNase A indicates that the hydrolysis reaction has to be considered formally as a special case of the transphosphorylation back reaction in which the R group of the R-OH substrate is just H. It is thus concluded that the 2',3'-cyclic phosphodiesters formed in the ribonuclease A reaction are true products of the transphosphorylation reaction and not intermediates as usually considered.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
333
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
207-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The role of 2',3'-cyclic phosphodiesters in the bovine pancreatic ribonuclease A catalysed cleavage of RNA: intermediates or products?
pubmed:affiliation
Departament de Bioquímica i Biologia Molecular, Facultat de Ciències, Universitat Autònoma de Barcelona, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't