Regulation of NAD+ glycohydrolase activity by NAD+-dependent auto-ADP-ribosylation
1996; Portland Press; Volume: 318; Issue: 3 Linguagem: Inglês
10.1042/bj3180903
ISSN1470-8728
AutoresMyung‐Kwan Han, Ji‐Young Lee, Yee-Sook Cho, Young Mi Song, Nyeon‐Hyoung An, Hyung-Rho Kim, Uh‐Hyun Kim,
Tópico(s)Neonatal Health and Biochemistry
ResumoNAD+ 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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