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. 1996 Sep 15;318(Pt 3):903–908. doi: 10.1042/bj3180903

Regulation of NAD+ glycohydrolase activity by NAD(+)-dependent auto-ADP-ribosylation.

M K Han 1, J Y Lee 1, Y S Cho 1, Y M Song 1, N H An 1, H R Kim 1, U H Kim 1
PMCID: PMC1217703  PMID: 8836136

Abstract

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.

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Selected References

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