Linked Life Data

18272369

Source:http://linkedlifedata.com/resource/pubmed/id/18272369

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2008-4-14
pubmed:abstractText
Thymidine phosphorylase (TP, EC 2.4.2.4) recognized the structure of the substrate with high specificity, via both the base and the ribosyl moieties. The replacement of 3'-OH of thymidine markedly influenced its catalytic activity with TP. The conversion of pyrimidine nucleosides with modified base moieties to the corresponding 1-phosphate form was poor. The leaving group activity decreased with an increase in aromaticity of the pyrimidine base moiety, because of increased difficulty in polarizing the base by the amino acids local to the active site. The replacement of 3' and 5' functional groups tended to decrease the reaction rate and the percentage conversion with TP. In particular the ribosyl 3' hydroxyl group was structurally important for the binding of the substrate by the enzyme. The kinetic assay clearly showed high K(m) and low V(max) values on replacing the 3' hydroxyl group with hydrogen.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1464-3391
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3866-70
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Kinetic parameters and recognition of thymidine analogues with varying functional groups by thymidine phosphorylase.
pubmed:affiliation
Department of Materials and Life Science, Shizuoka Institute of Science and Technology, 2200-2 Toyosawa, Fukuroi, Shizuoka 437-8555, Japan. a-hatano@ms.sist.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't