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Volumn 415, Issue 3, 2012, Pages 514-526

Structural studies of intermediates along the cyclization pathway of aplysia ADP-ribosyl cyclase

Author keywords

calcium signaling; cyclic ADP ribose; reaction mechanism; secondary messenger

Indexed keywords

ADENINE; ADENOSINE DIPHOSPHATE RIBOSYL CYCLASE; GUANINE; RIBOSE;

EID: 84855828493     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.11.022     Document Type: Article
Times cited : (7)

References (32)
  • 3
    • 0035033022 scopus 로고    scopus 로고
    • Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers
    • DOI 10.1146/annurev.pharmtox.41.1.317
    • Lee H.C. Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers Annu. Rev. Pharmacol. Toxicol. 41 2001 317 345 (Pubitemid 32385891)
    • (2001) Annual Review of Pharmacology and Toxicology , vol.41 , pp. 317-345
    • Lee, H.C.1
  • 5
    • 0023219685 scopus 로고
    • Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate
    • Clapper D.L., Walseth T.F., Dargie P.J., and Lee H.C. Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate J. Biol. Chem. 262 1987 9561 9568 (Pubitemid 17102610)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.20 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3    Hon Cheung Lee4
  • 6
    • 1942485783 scopus 로고    scopus 로고
    • 2+ stores: A perspective from cyclic ADP-ribose and NAADP
    • DOI 10.2174/1566524043360753
    • 2+ stores: a perspective from cyclic ADP-ribose and NAADP Curr. Mol. Med. 4 2004 227 237 (Pubitemid 38515234)
    • (2004) Current Molecular Medicine , vol.4 , Issue.3 , pp. 227-237
    • Lee, H.C.1
  • 7
    • 1942485497 scopus 로고    scopus 로고
    • Structure and enzymology of ADP-ribosyl cyclases: Conserved enzymes that produce multiple calcium mobilizing metabolites
    • DOI 10.2174/1566524043360708
    • Schuber F., and Lund F.E. Structure and enzymology of ADP-ribosyl cyclases: conserved enzymes that produce multiple calcium mobilizing metabolites Curr. Mol. Med. 4 2004 249 261 (Pubitemid 38515236)
    • (2004) Current Molecular Medicine , vol.4 , Issue.3 , pp. 249-261
    • Schuber, F.1    Lund, F.E.2
  • 8
    • 14844354701 scopus 로고
    • + into a calcium-mobilizing metabolite
    • + into a calcium-mobilizing metabolite Cell. Regul. 2 1991 203 209
    • (1991) Cell. Regul. , vol.2 , pp. 203-209
    • Lee, H.C.1    Aarhus, R.2
  • 9
    • 0032032393 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and calcium-induced calcium release regulate neurotransmitter release at a cholinergic synapse of Aplysia
    • DOI 10.1111/j.1469-7793.1998.405bt.x
    • Mothet J.P., Fossier P., Meunier F.M., Stinnakre J., Tauc L., and Baux G. Cyclic ADP-ribose and calcium-induced calcium release regulate neurotransmitter release at a cholinergic synapse of Aplysia J. Physiol. 507 1998 405 414 (Pubitemid 28135192)
    • (1998) Journal of Physiology , vol.507 , Issue.2 , pp. 405-414
    • Mothet, J.-P.1    Fossier, P.2    Meunier, F.-M.3    Stinnakre, J.4    Tauc, L.5    Baux, G.6
  • 11
    • 0029858306 scopus 로고    scopus 로고
    • Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38
    • DOI 10.1038/nsb1196-957
    • Prasad G.S., McRee D.E., Stura E.A., Levitt D.G., Lee H.C., and Stout C.D. Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38 Nat. Struct. Biol. 3 1996 957 964 (Pubitemid 26398330)
    • (1996) Nature Structural Biology , vol.3 , Issue.11 , pp. 957-964
    • Prasad, G.S.1    McRee, D.E.2    Stura, E.A.3    Levitt, D.G.4    Lee, H.C.5    Stout, C.D.6
  • 13
    • 70350437285 scopus 로고    scopus 로고
    • Structural basis for enzymatic evolution from a dedicated ADP-ribosyl cyclase to a multifunctional NAD hydrolase
    • Liu Q., Graeff R., Kriksunov I.A., Jiang H., Zhang B., and Oppenheimer N. Structural basis for enzymatic evolution from a dedicated ADP-ribosyl cyclase to a multifunctional NAD hydrolase J. Biol. Chem. 284 2009 27637 27645
    • (2009) J. Biol. Chem. , vol.284 , pp. 27637-27645
    • Liu, Q.1    Graeff, R.2    Kriksunov, I.A.3    Jiang, H.4    Zhang, B.5    Oppenheimer, N.6
  • 14
    • 0028402138 scopus 로고
    • The crystal structure of cyclic ADP-ribose
    • Lee H.C., Aarhus R., and Levitt D. The crystal structure of cyclic ADP-ribose Nat. Struct. Biol. 1 1994 143 144
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 143-144
    • Lee, H.C.1    Aarhus, R.2    Levitt, D.3
  • 15
    • 58849105013 scopus 로고    scopus 로고
    • Conformational closure of the catalytic site of human CD38 induced by calcium
    • Liu Q., Graeff R., Kriksunov I.A., Lam C.M., Lee H.C., and Hao Q. Conformational closure of the catalytic site of human CD38 induced by calcium Biochemistry 47 2008 13966 13973
    • (2008) Biochemistry , vol.47 , pp. 13966-13973
    • Liu, Q.1    Graeff, R.2    Kriksunov, I.A.3    Lam, C.M.4    Lee, H.C.5    Hao, Q.6
  • 16
    • 34047231298 scopus 로고    scopus 로고
    • Structural basis for formation and hydrolysis of the calcium messenger cyclic ADP-ribose by human CD38
    • DOI 10.1074/jbc.M609093200
    • Liu Q., Kriksunov I.A., Graeff R., Lee H.C., and Hao Q. Structural basis for formation and hydrolysis of the calcium messenger cyclic ADP-ribose by human CD38 J. Biol. Chem. 282 2007 5853 5861 (Pubitemid 47093739)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5853-5861
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3    Hon, C.L.4    Hao, Q.5
  • 17
    • 24344490302 scopus 로고    scopus 로고
    • Crystal structure of human CD38 extracellular domain
    • DOI 10.1016/j.str.2005.05.012, PII S0969212605002388
    • Liu Q., Kriksunov I.A., Graeff R., Munshi C., Lee H.C., and Hao Q. Crystal structure of human CD38 extracellular domain Structure 13 2005 1331 1339 (Pubitemid 41262100)
    • (2005) Structure , vol.13 , Issue.9 , pp. 1331-1339
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3    Munshi, C.4    Hon, C.L.5    Hao, Q.6
  • 18
    • 33845936792 scopus 로고    scopus 로고
    • Structural basis for the mechanistic understanding of human CD38-controlled multiple catalysis
    • DOI 10.1074/jbc.M606365200
    • Liu Q., Kriksunov I.A., Graeff R., Munshi C., Lee H.C., and Hao Q. Structural basis for the mechanistic understanding of human CD38-controlled multiple catalysis J. Biol. Chem. 281 2006 32861 32869 (Pubitemid 46036841)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.43 , pp. 32861-32869
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3    Munshi, C.4    Hon, C.L.5    Hao, Q.6
  • 19
    • 53849148622 scopus 로고    scopus 로고
    • Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38
    • Liu Q., Kriksunov I.A., Jiang H., Graeff R., Lin H., Lee H.C., and Hao Q. Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38 Chem. Biol. 15 2008 1068 1078
    • (2008) Chem. Biol. , vol.15 , pp. 1068-1078
    • Liu, Q.1    Kriksunov, I.A.2    Jiang, H.3    Graeff, R.4    Lin, H.5    Lee, H.C.6    Hao, Q.7
  • 20
    • 34548317513 scopus 로고    scopus 로고
    • Catalysis-associated conformational changes revealed by human CD38 complexed with a non-hydrolyzable substrate analog
    • DOI 10.1074/jbc.M701653200
    • Liu Q., Kriksunov I.A., Moreau C., Graeff R., Potter B.V., Lee H.C., and Hao Q. Catalysis-associated conformational changes revealed by human CD38 complexed with a non-hydrolyzable substrate analog J. Biol. Chem. 282 2007 24825 24832 (Pubitemid 47347511)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24825-24832
    • Liu, Q.1    Kriksunov, I.A.2    Moreau, C.3    Graeff, R.4    Potter, B.V.L.5    Hon, C.L.6    Hao, Q.7
  • 21
    • 79251593960 scopus 로고    scopus 로고
    • Dynamic conformations of the CD38-mediated NAD cyclization captured in a single crystal
    • Zhang H., Graeff R., Chen Z., Zhang L., Lee H., and Hao Q. Dynamic conformations of the CD38-mediated NAD cyclization captured in a single crystal J. Mol. Biol. 405 2011 1070 1078
    • (2011) J. Mol. Biol. , vol.405 , pp. 1070-1078
    • Zhang, H.1    Graeff, R.2    Chen, Z.3    Zhang, L.4    Lee, H.5    Hao, Q.6
  • 22
    • 0030024344 scopus 로고    scopus 로고
    • Fluorescent analogs of cyclic ADP-ribose: Synthesis, spectral characterization, and use
    • Graeff R.M., Walseth T.F., Hill H.K., and Lee H.C. Fluorescent analogs of cyclic ADP-ribose: synthesis, spectral characterization, and use Biochemistry 35 1996 379 386
    • (1996) Biochemistry , vol.35 , pp. 379-386
    • Graeff, R.M.1    Walseth, T.F.2    Hill, H.K.3    Lee, H.C.4
  • 23
  • 25
    • 57449083063 scopus 로고    scopus 로고
    • Hierarchical and helical self-assembly of ADP-ribosyl cyclase into large-scale protein microtubes
    • Liu Q., Kriksunov I.A., Wang Z., Graeff R., Lee H.C., and Hao Q. Hierarchical and helical self-assembly of ADP-ribosyl cyclase into large-scale protein microtubes J. Phys. Chem. B 112 2008 14682 14686
    • (2008) J. Phys. Chem. B , vol.112 , pp. 14682-14686
    • Liu, Q.1    Kriksunov, I.A.2    Wang, Z.3    Graeff, R.4    Lee, H.C.5    Hao, Q.6
  • 26
    • 0034647497 scopus 로고    scopus 로고
    • Identification of the enzymatic active site of CD38 by site-directed mutagenesis
    • DOI 10.1074/jbc.M909365199
    • Munshi C., Aarhus R., Graeff R., Walseth T.F., Levitt D., and Lee H.C. Identification of the enzymatic active site of CD38 by site-directed mutagenesis J. Biol. Chem. 275 2000 21566 21571 (Pubitemid 30481862)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21566-21571
    • Munshi, C.1    Aarhus, R.2    Graeff, R.3    Walseth, T.F.4    Levitt, D.5    Lee, H.C.6
  • 27
    • 0027944850 scopus 로고
    • Enzymatic synthesis and characterizations of cyclic GDP-ribose. A procedure for distinguishing enzymes with ADP-ribosyl cyclase activity
    • Graeff R.M., Walseth T.F., Fryxell K., Branton W.D., and Lee H.C. Enzymatic synthesis and characterizations of cyclic GDP-ribose. A procedure for distinguishing enzymes with ADP-ribosyl cyclase activity J. Biol. Chem. 269 1994 30260 30267
    • (1994) J. Biol. Chem. , vol.269 , pp. 30260-30267
    • Graeff, R.M.1    Walseth, T.F.2    Fryxell, K.3    Branton, W.D.4    Lee, H.C.5
  • 28
    • 0028028257 scopus 로고
    • NAD hydrolysis: Chemical and enzymatic mechanisms
    • Oppenheimer N.J. NAD hydrolysis: chemical and enzymatic mechanisms Mol. Cell. Biochem. 138 1994 245 251
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 245-251
    • Oppenheimer, N.J.1


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