Inhibition of ADP-ribosylation of histone by diadenosine 5', 5"' -p (1), p(4)-tetraphosphate |
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| Authors: | Y Tanaka N Matsunami K Yoshihara |
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| Affiliation: | Department of Biochemistry, Nara Medical University, Shijo-cho, Kashihara, Nara, Japan |
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| Abstract: | Diadenosine 5′, 5?-p1, p4-tetraphosphate (Ap4A) strongly inhibited ADP-ribosylation reaction of histone by purified bovine thymus poly(ADP-ribose) polymerase. This compound showed a relatively weak inhibitory effect on Mg2+-dependent, enzyme-bound poly(ADP-ribose) synthesis. Among various adenine nucleotides tested, including several diadenosine nucleotides with varying phosphate chain length, Ap4A was the most effective inhibitor of the histone-modification reaction. Ap5A and Ap6A showed slightly lower inhibitory effect than Ap4A. Kinetic analysis of the inhibitor (Ap4A) with varying concentration of substrate (NAD+) revealed that this compound is a “mixed type inhibitor”, with a Ki value of 5.1 μM. |
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| Keywords: | Ap2A diadenosine 5′, 5?-p1, p2(di?) Ap3A -p1, p3(tri?) Ap4A p1, p4(tetra?) Ap5A -p1, p5(penta?) Ap6A -pl, p6(hexa)-phosphate pApp adenosine 5′-mono ppApp 5′-di- pppApp 5′-triphosphate 3′-diphosphate |
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