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

Blanka Szurmak | Zendy; Aleksandra WysłouchCieszyńska | Zendy; Małgorzata WszelakaRylik | Zendy; Wojciech Bal | Zendy; Marta Dobrzańska | Zendy

Open Access

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

Author(s) -

Blanka Szurmak,

Aleksandra WysłouchCieszyńska,

Małgorzata WszelakaRylik,

Wojciech Bal,

Marta Dobrzańska

Publication year - 2008

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2008_3173

Subject(s) - isothermal titration calorimetry , arabidopsis thaliana , chemistry , arabidopsis , enzyme , hydrolase , biochemistry , titration , gene , stereochemistry , microbiology and biotechnology , biology , mutant , inorganic chemistry

Asymmetrical diadenosine 5',5 "-(PP4)-P-1 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 present efficient overexpression and detailed biochemical characteristics of the AtNUDX25 protein encoded by the At1g30110 gene. Aided by the determination of the binding constants of Mn(AP(4)A) and Mg(Ap(4)A) complexes using isothermal titration calorimetry (ITC) we show that AtNUDX25 preferentially hydrolyzes Ap(4)A in the form of a Mn2+ complex.

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