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首页> 美国政府科技报告 >Covalent Binding of 4-Carbamoylbenzenediazonium Chloride to Deoxyguanine Bases of DNA Resulting in Apparent Irreversible Inhibition of Poly(adenosine didhosphoribose) Polymerase at the Nicotinamide Binding Site
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Covalent Binding of 4-Carbamoylbenzenediazonium Chloride to Deoxyguanine Bases of DNA Resulting in Apparent Irreversible Inhibition of Poly(adenosine didhosphoribose) Polymerase at the Nicotinamide Binding Site

机译：4-氨基甲酰基苯重氮氯化物与DNa的脱氧鸟嘌呤碱基的共价结合导致烟酰胺结合位点的聚（腺苷二磷酸核糖）聚合酶的表观不可逆抑制

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摘要

The poly (adenosinediphosphoribose) polymerase activity of isolated liver nuclei was inhibited by 4-carbamoylbenzenediazonium chloride, referred to as 4-diazoniobenzamide, an effect that was dependent on the time of incubation and the concentration of the diazonium compound, with inhibition following first-order kinetics. The inhibition was not reversed by re-isolation of nuclei and centrifugal washing, whereas the inhibition by benzamide or 4-amino-benzamide was completely reversible under these conditions. Simultaneous incubation of 4-diazoniobenzamide with benzamide prevented enzyme inhibition. The 4-diazoniobenzoic acid analogue was not inhibitory. The mechanism of action of 4-diazoniobenzamide was traced to a specific covalent binding to dGMP of DNA to form N2-((4-carbomoylphenyl) zao)-2'-deoxy-guanosine 5'-monophosphate. Coenzymic DNA, by tight association with the polymerase protein, fixes the -C(O)NH2 moiety of the adduct at the nicotinamide-binding site of the enzyme.

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