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Mutational analyses of human thymidine kinase 2 reveal key residues in ATP-Mg2+ binding and catalysis

Wang, Liya and Eriksson, Staffan (2022). Mutational analyses of human thymidine kinase 2 reveal key residues in ATP-Mg2+ binding and catalysis. Nucleosides, Nucleotides and Nucleic Acids. 41 :3 , 264-272
[Research article]

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Abstract

Mitochondrial thymidine kinase 2 (TK2) is an essential enzyme for mitochondrial dNTP synthesis in many tissues. Deficiency in TK2 activity causes devastating mitochondrial diseases. Here we investigated several residues involved in substrate binding and catalysis. We showed that mutations of Gln-110 and Glu-133 affected Mg2+ and ATP binding, and thus are crucial for TK2 function. Furthermore, mutations of Gln-110 and Tyr-141 altered the kinetic behavior, suggesting their involvement in substrate binding through conformational changes. Since the 3 D structure of TK2 is still unknown, and thus, the identification of key amino acids for TK2 function may help to explain how TK2 mutations cause mitochondrial diseases.

Authors/Creators:Wang, Liya and Eriksson, Staffan
Title:Mutational analyses of human thymidine kinase 2 reveal key residues in ATP-Mg2+ binding and catalysis
Series Name/Journal:Nucleosides, Nucleotides and Nucleic Acids
Year of publishing :2022
Volume:41
Number:3
Page range:264-272
Number of Pages:9
Publisher:TAYLOR AND FRANCIS INC
ISSN:1525-7770
Language:English
Publication Type:Research article
Article category:Scientific peer reviewed
Version:Published version
Copyright:Creative Commons: Attribution-Noncommercial-No Derivative Works 4.0
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Biochemistry and Molecular Biology
Keywords:thymidine kinase 2, mutagenesis, substrate binding, ATP, Mg2+ binding, enzyme kinetics
URN:NBN:urn:nbn:se:slu:epsilon-p-116661
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-116661
Additional ID:
Type of IDID
DOI10.1080/15257770.2021.2001005
Web of Science (WoS)000717365700001
ID Code:27537
Faculty:VH - Faculty of Veterinary Medicine and Animal Science
Department:(VH) > Dept. of Anatomy, Physiology and Biochemistry
Deposited By: SLUpub Connector
Deposited On:12 Apr 2022 15:37
Metadata Last Modified:12 Apr 2022 15:41

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