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Inhibition of terminal deoxynucleotidyl transferase by adenine dinucleotides
Author(s) -
Pandey V.N.,
Amrute S.B.,
Satav J.G.,
Modak M.J.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81492-8
Subject(s) - terminal deoxynucleotidyl transferase , chemistry , substrate (aquarium) , transferase , primer (cosmetics) , biochemistry , nucleotide , stereochemistry , enzyme , microbiology and biotechnology , biology , tunel assay , apoptosis , ecology , organic chemistry , gene
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.