Influence of phosphorylation of THR-3, SER-11, and SER-15 on deoxycytidine kinase activity and stability

Autor:	Angélique Arts, Caroline Smal, S Ntamashimikiro, E. Van Den Neste, Françoise Bontemps
Rok vydání:	2010
Předmět:	inorganic chemicals Threonine Deoxyribonucleosides macromolecular substances environment and public health Biochemistry Cell Line Structure-Activity Relationship Deoxycytidine Kinase Enzyme Stability Genetics Serine Humans Phosphorylation Site-directed mutagenesis chemistry.chemical_classification Chemistry Mutagenesis General Medicine Deoxycytidine kinase Molecular biology enzymes and coenzymes (carbohydrates) Enzyme Phosphoprotein Mutagenesis Site-Directed bacteria Molecular Medicine Nucleoside
Zdroj:	Nucleosides, nucleotidesnucleic acids. 29(4-6)
ISSN:	1532-2335
Popis:	Deoxycytidine kinase (dCK) is a key enzyme in the salvage of deoxyribonucleosides and in the activation of several anticancer and antiviral nucleoside analogues. We have recently shown that dCK is a phosphoprotein. Four in vivo phosphorylation sites were identified: Thr-3, Ser-11, Ser-15, and Ser-74. Site-directed mutagenesis demonstrated that phosphorylation of Ser-74, the major phosphorylated residue, strongly influences dCK activity in eucaryotic cells. Here, we show that phosphorylation of the three other sites, located in the N-terminal extremity of the protein, does not significantly modify dCK activity, but phosphorylation of Thr-3 could promote dCK stability.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5abffeebd8977edb68b665297c34cee4 https://pubmed.ncbi.nlm.nih.gov/20544527 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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