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Article: A unified mechanism of enzymatic synthesis of two calcium messengers: Cyclic ADP-ribose and NAADP

TitleA unified mechanism of enzymatic synthesis of two calcium messengers: Cyclic ADP-ribose and NAADP
Authors
Issue Date1999
PublisherWalter de Gruyter GmbH & Co KG. The Journal's web site is located at http://www.degruyter.de/journals/bc
Citation
Biological Chemistry, 1999, v. 380 n. 7-8, p. 785-793 How to Cite?
AbstractCyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) mobilize Ca2+ from two different types of intracellular stores and through completely independent mechanisms. The two Ca2+ messengers are also structurally distinct. cADPR is a cyclic nucleotide derived from NAD, while NAADP is a linear metabolite of NADP. Systems responsive to these two novel signaling molecules are widespread among eukaryotes and include protozoan, plant, invertebrate, mammalian as well as human cells. Despite their functional and structural differences, cADPR and NAADP are sibling messengers synthesized by a single enzyme, ADP-ribosyl cyclase. In this article the recent progress in understanding the physiological roles of cADPR and NAADP is briefly reviewed. A unified mechanism of catalysis is also proposed, which takes into consideration the crystallographic structure of ADP-ribosyl cyclase and accounts for its novel multi-functionality.
Persistent Identifierhttp://hdl.handle.net/10722/171665
ISSN
2015 Impact Factor: 2.71
2015 SCImago Journal Rankings: 1.607
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_US
dc.date.accessioned2012-10-30T06:16:14Z-
dc.date.available2012-10-30T06:16:14Z-
dc.date.issued1999en_US
dc.identifier.citationBiological Chemistry, 1999, v. 380 n. 7-8, p. 785-793en_US
dc.identifier.issn1431-6730en_US
dc.identifier.urihttp://hdl.handle.net/10722/171665-
dc.description.abstractCyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) mobilize Ca2+ from two different types of intracellular stores and through completely independent mechanisms. The two Ca2+ messengers are also structurally distinct. cADPR is a cyclic nucleotide derived from NAD, while NAADP is a linear metabolite of NADP. Systems responsive to these two novel signaling molecules are widespread among eukaryotes and include protozoan, plant, invertebrate, mammalian as well as human cells. Despite their functional and structural differences, cADPR and NAADP are sibling messengers synthesized by a single enzyme, ADP-ribosyl cyclase. In this article the recent progress in understanding the physiological roles of cADPR and NAADP is briefly reviewed. A unified mechanism of catalysis is also proposed, which takes into consideration the crystallographic structure of ADP-ribosyl cyclase and accounts for its novel multi-functionality.en_US
dc.languageengen_US
dc.publisherWalter de Gruyter GmbH & Co KG. The Journal's web site is located at http://www.degruyter.de/journals/bcen_US
dc.relation.ispartofBiological Chemistryen_US
dc.subject.meshAdp-Ribosyl Cyclaseen_US
dc.subject.meshAdenosine Diphosphate Ribose - Analogs & Derivatives - Biosynthesis - Chemistry - Physiologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cden_US
dc.subject.meshAntigens, Cd38en_US
dc.subject.meshAntigens, Differentiation - Metabolismen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshCatalysisen_US
dc.subject.meshCyclic Adp-Riboseen_US
dc.subject.meshHumansen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshNad+ Nucleosidase - Metabolismen_US
dc.subject.meshNadp - Analogs & Derivatives - Biosynthesis - Chemistry - Physiologyen_US
dc.titleA unified mechanism of enzymatic synthesis of two calcium messengers: Cyclic ADP-ribose and NAADPen_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.doi10.1515/BC.1999.098en_US
dc.identifier.pmid10494827-
dc.identifier.scopuseid_2-s2.0-0032830476en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032830476&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume380en_US
dc.identifier.issue7-8en_US
dc.identifier.spage785en_US
dc.identifier.epage793en_US
dc.identifier.isiWOS:000082438200008-
dc.publisher.placeGermanyen_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US

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