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© Institut Pasteur
Cristaux de cellulase, enzyme purifiée de Clostridium thermocellum permettant la digestion de la cellulose. Image colorisée.
Publication : Nucleic acids research. Supplement (2001)

Substrate recognition by the human MTH1 protein

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nucleic acids research. Supplement (2001) - 01 Jan 2002

Kamiya H, Dugué L, Yakushiji H, Pochet S, Nakabeppu Y, Harashima H

Link to Pubmed [PMID] – 12903117

Nucleic Acids Res. Suppl. 2002;(2):85-6

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.

http://www.ncbi.nlm.nih.gov/pubmed/12903117