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

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...

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Published inBiochemical journal Vol. 318 ( Pt 3); no. 3; pp. 903 - 908
Main Authors Han, M K, Lee, J Y, Cho, Y S, Song, Y M, An, N H, Kim, H R, Kim, U H
Format Journal Article
LanguageEnglish
Published England 15.09.1996
Subjects
Adenosine Diphosphate Ribose - metabolism
Animals
Binding Sites
Cysteine - chemistry
Erythrocytes - enzymology
In Vitro Techniques
Kinetics
Molecular Weight
NAD - metabolism
NAD+ Nucleosidase - antagonists & inhibitors
NAD+ Nucleosidase - chemistry
NAD+ Nucleosidase - metabolism
Rabbits
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Summary: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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ISSN:0264-6021
1470-8728
DOI:10.1042/bj3180903