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Article: Wide distribution of an enzyme that catalyzes the hydrolysis of cyclic ADP-ribose

TitleWide distribution of an enzyme that catalyzes the hydrolysis of cyclic ADP-ribose
Authors
Issue Date1993
Citation
Biochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1993, v. 1164 n. 1, p. 68-74 How to Cite?
AbstractCyclic ADP-ribose (cADPR) is a metabolite of NAD+ that is as effective as inositol trisphosphate in mobilizing intracellular Ca2+ stores. Its synthesizing enzyme, ADP-ribosyl cyclase, has been shown to be present in mammalian and invertebrate tissues. In this study we identity another widely-distributed enzyme that can hydrolyze cADPR to ADP-ribose. Incubation of cADPR with brain extracts resulted in progressive decrease in its Ca2+ mobilizing activity. The degradation of cADPR was catalyzed by a heat-labile protein factor in the brain extracts. Analysis by HPLC indicated a single degradation product was produced in equal molar quantity and that it has identical elution time as ADP-ribose. Proton NMR confirmed that the product was ADP-ribose. The degradation enzyme had a Michaelis constant of 0.16 mM and a broad pH maximum around neutrality. Centrifugation studies of the total brain extracts showed that the degradation activity was membrane-bound. Survey of tissues from various animals established that both the degradation and the synthesizing enzyme of cADPR were widely distributed from mammals to invertebrates. Since the degradation enzyme hydrolyzes an unique linkage between the adenine group and the terminal ribosyl moiety of cADPR, we propose to call it cyclic ADP-ribose hydrolase.
Persistent Identifierhttp://hdl.handle.net/10722/171574
ISSN
2004 Impact Factor: 3.079
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_US
dc.contributor.authorAarhus, Ren_US
dc.date.accessioned2012-10-30T06:15:45Z-
dc.date.available2012-10-30T06:15:45Z-
dc.date.issued1993en_US
dc.identifier.citationBiochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1993, v. 1164 n. 1, p. 68-74en_US
dc.identifier.issn0167-4838en_US
dc.identifier.urihttp://hdl.handle.net/10722/171574-
dc.description.abstractCyclic ADP-ribose (cADPR) is a metabolite of NAD+ that is as effective as inositol trisphosphate in mobilizing intracellular Ca2+ stores. Its synthesizing enzyme, ADP-ribosyl cyclase, has been shown to be present in mammalian and invertebrate tissues. In this study we identity another widely-distributed enzyme that can hydrolyze cADPR to ADP-ribose. Incubation of cADPR with brain extracts resulted in progressive decrease in its Ca2+ mobilizing activity. The degradation of cADPR was catalyzed by a heat-labile protein factor in the brain extracts. Analysis by HPLC indicated a single degradation product was produced in equal molar quantity and that it has identical elution time as ADP-ribose. Proton NMR confirmed that the product was ADP-ribose. The degradation enzyme had a Michaelis constant of 0.16 mM and a broad pH maximum around neutrality. Centrifugation studies of the total brain extracts showed that the degradation activity was membrane-bound. Survey of tissues from various animals established that both the degradation and the synthesizing enzyme of cADPR were widely distributed from mammals to invertebrates. Since the degradation enzyme hydrolyzes an unique linkage between the adenine group and the terminal ribosyl moiety of cADPR, we propose to call it cyclic ADP-ribose hydrolase.en_US
dc.languageengen_US
dc.relation.ispartofBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymologyen_US
dc.subject.meshAdp-Ribosyl Cyclaseen_US
dc.subject.meshAdenosine Diphosphate Ribose - Analogs & Derivatives - Biosynthesis - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cden_US
dc.subject.meshAntigens, Cd38en_US
dc.subject.meshAntigens, Differentiation - Analysis - Metabolismen_US
dc.subject.meshBrain - Embryology - Enzymologyen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshChick Embryoen_US
dc.subject.meshCyclic Adp-Riboseen_US
dc.subject.meshDogsen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshModels, Chemicalen_US
dc.subject.meshN-Glycosyl Hydrolases - Analysis - Metabolismen_US
dc.subject.meshNad - Metabolismen_US
dc.subject.meshNiacinamide - Metabolismen_US
dc.subject.meshSea Urchinsen_US
dc.titleWide distribution of an enzyme that catalyzes the hydrolysis of cyclic ADP-riboseen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0167-4838(93)90113-6en_US
dc.identifier.pmid8518298-
dc.identifier.scopuseid_2-s2.0-0027230589en_US
dc.identifier.volume1164en_US
dc.identifier.issue1en_US
dc.identifier.spage68en_US
dc.identifier.epage74en_US
dc.identifier.isiWOS:A1993LK41400010-
dc.identifier.scopusauthoridLee, HC=26642959100en_US
dc.identifier.scopusauthoridAarhus, R=6701339421en_US

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