Source:http://linkedlifedata.com/resource/pubmed/id/11883607
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2002-3-8
|
pubmed:abstractText |
A DNA glycosylase specific for UV radiation-induced pyrimidine dimers has been identified from the Chlorella virus Paramecium Bursaria Chlorella virus-1. This enzyme (Chlorella virus pyrimidine dimer glycosylase [cv-pdg]) exhibits a 41% amino acid identity with endonuclease V from bacteriophage T4 (T4 pyrimidine dimer glycosylase [T4-pdg]), which is also specific for pyrimidine dimers. However, cv-pdg possesses a higher catalytic efficiency and broader substrate specificity than T4-pdg. The latter excises 4,6-diamino-5-formamidopyrimidine (FapyAde), a UV radiation- and hydroxyl radical-induced monomeric product of adenine in DNA. Using gas chromatography-isotope-dilution mass spectrometry and y-irradiated DNA, we show in this work that cv-pdg also displays a catalytic activity for excision of FapyAde and, in addition, it excises 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua). Kinetic data show that FapyAde is a better substrate for cv-pdg than FapyGua. On the other hand, cv-pdg possesses a greater efficiency for the extension of FapyAde than T4-pdg. These two enzymes exhibit different substrate specificities despite substantial structural similarities.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2,6-diamino-4-hydroxy-5-formamidopyr...,
http://linkedlifedata.com/resource/pubmed/chemical/4,6-diamino-5-N-formamidopyrimidine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Glycosylases,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyl Radical,
http://linkedlifedata.com/resource/pubmed/chemical/N-Glycosyl Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrimidine Dimers,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrimidines,
http://linkedlifedata.com/resource/pubmed/chemical/deoxyribopyrimidine endonucleosidase
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0031-8655
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
75
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
85-91
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:11883607-Chlorella,
pubmed-meshheading:11883607-DNA Damage,
pubmed-meshheading:11883607-DNA Glycosylases,
pubmed-meshheading:11883607-DNA Repair,
pubmed-meshheading:11883607-Hydroxyl Radical,
pubmed-meshheading:11883607-N-Glycosyl Hydrolases,
pubmed-meshheading:11883607-Pyrimidine Dimers,
pubmed-meshheading:11883607-Pyrimidines,
pubmed-meshheading:11883607-Substrate Specificity,
pubmed-meshheading:11883607-Ultraviolet Rays
|
pubmed:year |
2002
|
pubmed:articleTitle |
Chlorella virus pyrimidine dimer glycosylase excises ultraviolet radiation- and hydroxyl radical-induced products 4,6-diamino-5-formamidopyrimidine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine from DNA.
|
pubmed:affiliation |
Chemical Science and Technology Laboratory, National Institute of Standards and Technology, Gaithersburg, MD, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|