Kinetic and structural characterization of an alternatively spliced variant of human mitochondrial 5'(3')-deoxyribonucleotidase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F15%3A00435125" target="_blank" >RIV/61388963:_____/15:00435125 - isvavai.cz</a>
Alternative codes found
RIV/68378050:_____/15:00435125
Result on the web
<a href="http://dx.doi.org/10.3109/14756366.2013.879577" target="_blank" >http://dx.doi.org/10.3109/14756366.2013.879577</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3109/14756366.2013.879577" target="_blank" >10.3109/14756366.2013.879577</a>
Alternative languages
Result language
angličtina
Original language name
Kinetic and structural characterization of an alternatively spliced variant of human mitochondrial 5'(3')-deoxyribonucleotidase
Original language description
Abstract Human mitochondrial 5'(3')-deoxyribonucleotidase (mdN) catalyzes dephosphorylation of nucleoside monophosphates, and thus helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Mature mdN is a 23-kDa dimeric protein with highest expression levels in the heart, brain and skeletal muscle. We have identified an alternative splice variant of the mdN gene containing an 18-nucleotide insertion encoding 6 amino acids (GKWPAT) at the 3'-end of the penultimate exon 4. We recombinantly expressed this enzyme variant and characterized its biochemical and kinetic properties as well as its three-dimensional structure. Our high-resolution (1.27??) crystal structure revealed that the insertion forms a loop located in the vicinity of the active site pocket and affects enzyme kinetic parameters as well as protein thermal stability.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Enzyme Inhibition and Medicinal Chemistry
ISSN
1475-6366
e-ISSN
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Volume of the periodical
30
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
6
Pages from-to
63-68
UT code for WoS article
000347956500010
EID of the result in the Scopus database
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