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首页> 美国政府科技报告 >Mechanisms of Poly(ADP-ribose) polymerase Catalysis; Mono-ADP-ribosylation of Poly(ADP-ribose) polymerase at Nanomolar Concentrations of NAD
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Mechanisms of Poly(ADP-ribose) polymerase Catalysis; Mono-ADP-ribosylation of Poly(ADP-ribose) polymerase at Nanomolar Concentrations of NAD

机译：聚（aDp-核糖）聚合酶催化机制;纳摩尔浓度的NaD的聚（aDp-核糖）聚合酶的单-aDp-核糖基化

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Calf thymus and rat liver poly (adenosine diphosphate-ribose) polymerase enzymes, and the polymerase present in extracts of rat liver nuclei synthesize unstable mono-ADP-ribose adducts at 100 nanomolar or lower nicotinamide-adenine dinucleotide concentrations. The isolated enzyme-mono-ADP-ribose adduct hydrolyses to ADP-ribose and enzyme protein at pH values slightly above 7.0 indicating a continuous release of ADP-ribose from NAD through this enzyme-bound intermediate under physiological conditions. Hydroxylamine at pH 7.0 hydrolyses the mono-ADP-ribose enzyme adduct. Desamino and some other homologs at nanomolar concentrations act as 'forward' activators of the initiating mono-ADP-ribosylation reaction. These NAD analogs at micomolar concentrations do not affect polymer formation that takes place at micromolar NAD concentrations. Benzamides at nanomolar concentrations also activate mono-ADP-ribosylation of the enzyme, but at higher concentrations inhibit enlongation at micromolar as substrate. In nuclei the enzyme molecule extensively auto-ADP-ribosylates itself, whereas histones are trans-ADP-ribosylated to a much lower extent. The unstable mono-ADP-ribose enzyme adduct represents an initiator intermediate in poly ADP-ribosylation. Reprints.

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