通过NAD(+)依赖性自身ADP-核糖基化对NAD+糖水解酶活性的调节。
Regulation of NAD+ glycohydrolase activity by NAD(+)-dependent auto-ADP-ribosylation.
作者信息
Han M K, Lee J Y, Cho Y S, Song Y M, An N H, Kim H R, Kim U H
机构信息
Department of Biochemistry, Chonbuk National University Medical School, Chonju, Korea.
出版信息
Biochem J. 1996 Sep 15;318 ( Pt 3)(Pt 3):903-8. doi: 10.1042/bj3180903.
NAD+ glycohydrolase (NADase; EC 3.2.2.5) is an enzyme that catalyses hydrolysis of NAD+ to produce ADP-ribose and nicotinamide. Its physiological role and the regulation of its enzymic activity have not been fully elucidated. In the present study, the mechanism of self-inactivation of NADase by its substrate, NAD+, was investigated by using intact rabbit erythrocytes and purified NADase. Our results suggest that inactivation of NADase was due an auto-ADP-ribosylation reaction. ADP-ribosylated NADase of rabbit erythrocytes was deADP-ribosylated when incubated without NAD+, and thus enzyme activity was simultaneously restored. These findings suggest that reversible auto-ADP-ribosylation of NADase might regulate the enzyme's activity in vivo.
NAD+糖水解酶（NADase；EC 3.2.2.5）是一种催化NAD+水解生成ADP-核糖和烟酰胺的酶。其生理作用及其酶活性的调节尚未完全阐明。在本研究中，通过使用完整的兔红细胞和纯化的NADase，研究了NADase被其底物NAD+自失活的机制。我们的结果表明，NADase的失活是由于自动ADP-核糖基化反应。兔红细胞的ADP-核糖基化NADase在无NAD+的情况下孵育时会发生去ADP-核糖基化，因此酶活性同时恢复。这些发现表明，NADase的可逆自动ADP-核糖基化可能在体内调节该酶的活性。
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