Inhibition of ADP-ribosylation of histone by diadenosine 5′, 5‴-p1, p4-tetraphosphate
作者： Yasuharu Tanaka , Norisada Matsunami , Koichiro Yoshihara
DOI: 10.1016/0006-291X(81)91240-7
关键词: Ap4A 、 Biochemistry 、 Nucleotide 、 Polymerase 、 NAD+ kinase 、 Adenine nucleotide 、 Molecular biology 、 Phosphate 、 Chemistry 、 Substrate (chemistry) 、 ADP-ribosylation
摘要: Abstract Diadenosine 5′, 5‴-p 1 , p 4 -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 Mg 2+ -dependent, enzyme-bound synthesis. Among various adenine nucleotides tested, including several diadenosine with varying phosphate chain length, Ap4A was the most effective inhibitor histone-modification reaction. Ap5A and Ap6A slightly lower than Ap4A. Kinetic analysis concentration substrate (NAD + ) revealed that this is “mixed type inhibitor”, Ki value 5.1 μM.
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