Substrate recognition by the human MTH1 protein.

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

研究成果: Contribution to journalConference article

2 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)85-86
ページ数2
ジャーナルNucleic Acids Research
Supplemant
No 2
DOI
出版ステータス出版済み - 2002
外部発表はい

All Science Journal Classification (ASJC) codes

  • 医学(全般)

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