A diadenosine 5',5''-P1P4 tetraphosphate (Ap4A) hydrolase from Arabidopsis thaliana that is activated preferentially by Mn2+ ions.

@article{Szurmak2008AD5,
  title={A diadenosine 5',5''-P1P4 tetraphosphate (Ap4A) hydrolase from Arabidopsis thaliana that is activated preferentially by Mn2+ ions.},
  author={Blanka Szurmak and Aleksandra Wysłouch-Cieszyńska and Małgorzata Wszelaka-Rylik and Wojciech Bal and Marta Dobrzańska},
  journal={Acta biochimica Polonica},
  year={2008},
  volume={55 1},
  pages={151-60}
}
Asymmetrical diadenosine 5',5''-P(1)P(4) tetraphosphate (Ap(4)A) hydrolases are key enzymes controlling the in vivo concentration of Ap(4)A--an important signaling molecule involved in regulation of DNA replication and repair, signaling in stress response and apoptosis. Sequence homologies indicate that the genome of the model plant Arabidopsis thaliana contains at least three open reading frames encoding presumptive Ap(4)A hydrolases: At1g30110, At3g10620, and At5g06340. In this work we… CONTINUE READING
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