Substrate recognition by the human MTH1 protein.

Hiroyuki Kamiya, Laurence Dugué, Hiroyuki Yakushiji, Sylvie Pochet, Yusaku Nakabeppu, Hideyoshi Harashima

Research output: Contribution to journalConference article

2 Citations (Scopus)

Abstract

A nucleotide pool sanitizing enzyme, the human MTH1 protein, hydrolyzes 2-hydroxy-dATP, 8-hydroxy-dATP, and 8-hydroxyd-GTP. To examine the substrate recognition mechanism of the MTH1 protein, ten nucleotide analogs (8-bromo-dATP, 8-bromod-GTP, deoxyisoinosine triphosphate, 8-hydroxy-dITP, 2-aminopurine-deoxyriboside triphosphate, 2-amino-dATP, deoxyxanthosine triphosphate, deoxyoxanosine triphosphate, dITP, and dUTP) were incubated with the protein. Of these, the former five nucleotides were hydrolyzed with various efficiencies. This results suggests the importance of the anti/syn-conformation and the functional groups on the 2 and 6-positions of the purine ring.

Original languageEnglish
Pages (from-to)85-86
Number of pages2
JournalNucleic Acids Research
VolumeSupplemant
Issue numberNo 2
DOIs
Publication statusPublished - 2002

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    Kamiya, H., Dugué, L., Yakushiji, H., Pochet, S., Nakabeppu, Y., & Harashima, H. (2002). Substrate recognition by the human MTH1 protein. Nucleic Acids Research, Supplemant(No 2), 85-86. https://doi.org/10.1093/nass/2.1.85