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PMID: 8836136 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The Biochemical journal ·Vol. 318 ( Pt 3) ·1996-09-15 ·Pages 903-8

Han MK, Lee JY, Cho YS, Song YM, An NH, Kim HR, Kim UH

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.

MeSH Terms
Adenosine Diphosphate Ribose/metabolism Animals Binding Sites Cysteine/chemistry Erythrocytes/enzymology In Vitro Techniques Kinetics Molecular Weight NAD/metabolism NAD+ Nucleosidase/antagonists & inhibitors,chemistry,metabolism Rabbits
Chemicals
NAD Adenosine Diphosphate Ribose NAD+ Nucleosidase Cysteine
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Han M K
Department of Biochemistry, Chonbuk National University Medical School, Chonju, Korea.
Lee J Y
Cho Y S
Song Y M
An N H
Kim H R
Kim U H
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj3180903
Published
1996-09-15
Pages
903-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1217703
Subset
IM
External Links
PubMed source DOI: 10.1042/bj3180903 PMC Full Text View journal details
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