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Article: ADP-ribosyl cyclase and CD38: Multi-functional enzymes in Ca+2 signaling

TitleADP-ribosyl cyclase and CD38: Multi-functional enzymes in Ca+2 signaling
Authors
KeywordsSpecies Index: Aplysia
Issue Date1997
PublisherSpringer New York LLC
Citation
Advances In Experimental Medicine And Biology, 1997, v. 419, p. 411-419 How to Cite?
AbstractMobilization of internal Ca+2 is an important signaling mechanism in cells. In addition to the inositol trisphosphate pathway, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide (NAADP) have been shown to mobilize Ca+2 via independent mechanisms. Although the structures of cADPR and NAADP are totally distinct, both nucleotides can be synthesized by ADP- ribosyl cyclase or CD38, a lymphocyte antigen. Both enzymes cyclize NAD to cADPR. In the presence of nicotinic acid the two enzymes catalyze a base exchange reaction resulting in the synthesis of NAADP from NADP. The switch between these two modes of catalysis is regulated by pH. Furthermore, both enzymes can also cyclic nicotinamide guanine dinucleotide (NGD) to produce a fluorescent product, cyclic GDP-ribose (cGDPR), which has a site of cyclization different from cADPR. A model is proposed to account for the multi-functionality of these enzymes. In order to be able to verify the model, a soluble ADP-ribosyl cyclase has been crystallized and X-ray diffraction shows that it is a dimer. Solution of the crystal structure of the cyclase should provide valuable insight into the structural features necessary for its multiple catalytic functions.
Persistent Identifierhttp://hdl.handle.net/10722/132575
ISSN
2015 Impact Factor: 1.953
2015 SCImago Journal Rankings: 0.887
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_HK
dc.contributor.authorGraeff, RMen_HK
dc.contributor.authorWalseth, TFen_HK
dc.date.accessioned2011-03-28T09:26:27Z-
dc.date.available2011-03-28T09:26:27Z-
dc.date.issued1997en_HK
dc.identifier.citationAdvances In Experimental Medicine And Biology, 1997, v. 419, p. 411-419en_HK
dc.identifier.issn0065-2598en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132575-
dc.description.abstractMobilization of internal Ca+2 is an important signaling mechanism in cells. In addition to the inositol trisphosphate pathway, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide (NAADP) have been shown to mobilize Ca+2 via independent mechanisms. Although the structures of cADPR and NAADP are totally distinct, both nucleotides can be synthesized by ADP- ribosyl cyclase or CD38, a lymphocyte antigen. Both enzymes cyclize NAD to cADPR. In the presence of nicotinic acid the two enzymes catalyze a base exchange reaction resulting in the synthesis of NAADP from NADP. The switch between these two modes of catalysis is regulated by pH. Furthermore, both enzymes can also cyclic nicotinamide guanine dinucleotide (NGD) to produce a fluorescent product, cyclic GDP-ribose (cGDPR), which has a site of cyclization different from cADPR. A model is proposed to account for the multi-functionality of these enzymes. In order to be able to verify the model, a soluble ADP-ribosyl cyclase has been crystallized and X-ray diffraction shows that it is a dimer. Solution of the crystal structure of the cyclase should provide valuable insight into the structural features necessary for its multiple catalytic functions.en_HK
dc.languageengen_US
dc.publisherSpringer New York LLCen_US
dc.relation.ispartofAdvances in Experimental Medicine and Biologyen_HK
dc.subjectSpecies Index: Aplysiaen_US
dc.titleADP-ribosyl cyclase and CD38: Multi-functional enzymes in Ca+2 signalingen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, HC: leehc@hku.hken_HK
dc.identifier.emailGraeff, RM: graeffr@hku.hken_HK
dc.identifier.authorityLee, HC=rp00545en_HK
dc.identifier.authorityGraeff, RM=rp01464en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid9193683-
dc.identifier.scopuseid_2-s2.0-0030990780en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030990780&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume419en_HK
dc.identifier.spage411en_HK
dc.identifier.epage419en_HK
dc.identifier.isiWOS:A1997BH84G00053-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLee, HC=26642959100en_HK
dc.identifier.scopusauthoridGraeff, RM=7003614053en_HK
dc.identifier.scopusauthoridWalseth, TF=7005424273en_HK

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