Substrate recognition by the human MTH1 protein | Zendy

Hiroyuki Kamiya | Zendy; Laura Dugué | Zendy; Hiroyuki Yakushiji | Zendy; Sylvie Pochet | Zendy; Yusaku Nakabeppu | Zendy; Hideyoshi Harashima | Zendy

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Substrate recognition by the human MTH1 protein

Author(s) -

Hiroyuki Kamiya,

Laura Dugué,

Hiroyuki Yakushiji,

Sylvie Pochet,

Yusaku Nakabeppu,

Hideyoshi Harashima

Publication year - 2002

Publication title -

nucleic acids symposium series

Language(s) - English

Resource type - Journals

eISSN - 1746-8272

pISSN - 0261-3166

DOI - 10.1093/nass/2.1.85

Subject(s) - nucleotide , gtp' , purine , biochemistry , adenosine triphosphate , enzyme , chemistry , substrate (aquarium) , guanosine triphosphate , hydrolysis , atp hydrolysis , biology , atpase , ecology , gene

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.

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