Inhibition of terminal deoxynucleotidyl transferase by adenine dinucleotides

FEBS Letters

Modak, M.J.¹  Amrute, S.B.¹  Pandey, V.N.¹  Satav, J.G.¹ 

[1] Department of Biochemistry, UMDNJ-New Jersey Medical School, 100 Bergen Street, Newark, NJ 07103-2757, USA

关键词: Terminal deoxynucleotidyltransferase;    Adenine dinucleotide inhibitor;    Ap2A;    Ap3A;    Ap4A;    Ap5A and Ap6A;    diadenosine (5'-5')di-;    tri-;    tetra-;    penta- and hexa-phosphate;    respectively;    TdT;    terminal deoxynucleotidyltransferase;    dNTP;    deoxynucleoside triphosphate;   

DOI  :  10.1016/0014-5793(87)81492-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Terminal deoxynucleotidyltransferase (TdT) exhibits strong sensitivity to ATP and its dinucleotide analogues, Ap2A, Ap3A, Ap4A, Ap5A and Ap6A. Similar to ATP, all of the dinucleotides appear to be competitive inhibitors of TdT catalysis with respect to substrate deoxynucleoside triphosphates and effectively block the UV-mediated substrate cross-linking to TdT. Among the various dinucleotides, Ap5A and Ap6A (diadenosine 5'-5' penta- and hexaphosphate, respectively) are significantly more effective than dinucleotides containing 2, 3 or 4 phosphate backbones. Furthermore, Ap5A is found to be the only dinucleotide which has reactivity at both substrate- and primer-binding domains in TdT.

【 授权许可】

Unknown