Regulation of NAD+ glycohydrolase activity by NAD+-dependent auto-ADP-ribosylation
نویسندگان
چکیده
منابع مشابه
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 substrate, NAD+, was investigated by using intact rabbit erythrocytes and purified NADase. Our re...
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Erythrocytic NADH methemoglobin diaphorase acquires NADH-dichlorophenolindophenol diaphorase activity when enzyme-associated NAD is removed. This transformation is reversible and can be mediated by membrane NAD glycohydrolase (EC 3.2.2.5) in hemolysates as well as in intact cells exposed to hydrogen peroxide. It is abolished either in NADH methemoglobin diaphorase deficiency or in NAD(P) glycoh...
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When permeabilized hamster fibroblasts were incubated with 4 mM-NAD+, the substrate for poly(ADP-ribose) polymerase, RNA polymerase I activity was inhibited by about 85%. This inhibition was not relieved by prior incubation of cells with 3-aminobenzamide, a potent inhibitor of the poly(ADP-ribose) polymerase. Digestion of cells with pancreatic deoxyribonuclease I resulted in the inhibition of R...
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NAD glycohydrolases (NADases) catalyze the hydrolysis of NAD to ADP-ribose and nicotinamide. Although many members of the NADase family, including ADP-ribosyltransferases, have been cloned and characterized, the structure and function of NADases with pure hydrolytic activity remain to be elucidated. Here, we report the structural and functional characterization of a novel NADase from rabbit ret...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1996
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3180903