메뉴 건너뛰기




Volumn 398, Issue 3, 2010, Pages 500-505

2',3'-cAMP hydrolysis by metal-dependent phosphodiesterases containing DHH, EAL, and HD domains is non-specific: Implications for PDE screening

Author keywords

2',3' cAMP; Hydrolysis; Non specific; Phosphodiesterase

Indexed keywords

ADENOSINE 2' PHOSPHATE; ADENOSINE 2',3' PHOSPHATE; ADENOSINE 3' PHOSPHATE; BIS(4 NITROPHENYL) PHOSPHATE; PHOSPHODIESTERASE;

EID: 77955271184     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.06.107     Document Type: Article
Times cited : (28)

References (36)
  • 1
    • 0027430772 scopus 로고
    • The role of 2',3'-cyclic phosphodiesters in the bovine pancreatic ribonuclease A catalysed cleavage of RNA: intermediates or products?
    • Cuchillo C.M., Pares X., Guasch A., Barman T., Travers F., Nogues M.V. The role of 2',3'-cyclic phosphodiesters in the bovine pancreatic ribonuclease A catalysed cleavage of RNA: intermediates or products?. FEBS Lett. 1993, 333:207-210.
    • (1993) FEBS Lett. , vol.333 , pp. 207-210
    • Cuchillo, C.M.1    Pares, X.2    Guasch, A.3    Barman, T.4    Travers, F.5    Nogues, M.V.6
  • 2
    • 62449261216 scopus 로고    scopus 로고
    • Identification and quantification of 2',3'-cAMP release by the kidney
    • Ren J., Mi Z., Stewart N.A., Jackson E.K. Identification and quantification of 2',3'-cAMP release by the kidney. J. Pharmacol. Exp. Ther. 2009, 328:855-865.
    • (2009) J. Pharmacol. Exp. Ther. , vol.328 , pp. 855-865
    • Ren, J.1    Mi, Z.2    Stewart, N.A.3    Jackson, E.K.4
  • 3
    • 70450233473 scopus 로고    scopus 로고
    • Extracellular 2',3'-cAMP is a source of adenosine
    • Jackson E.K., Ren J., Mi Z. Extracellular 2',3'-cAMP is a source of adenosine. J. Biol. Chem. 2009, 284:33097-33106.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33097-33106
    • Jackson, E.K.1    Ren, J.2    Mi, Z.3
  • 4
    • 0003448878 scopus 로고
    • Hydrolysis of ribonucleoside 2',3'-cyclic phosphates by a diesterase from brain
    • Drummond G.I., Iyer N.T., Keith J. Hydrolysis of ribonucleoside 2',3'-cyclic phosphates by a diesterase from brain. J. Biol. Chem. 1962, 237:3535-3539.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3535-3539
    • Drummond, G.I.1    Iyer, N.T.2    Keith, J.3
  • 5
    • 38649108114 scopus 로고    scopus 로고
    • Mammalian 2',3' cyclic nucleotide phosphodiesterase (CNP) can function as a tRNA splicing enzyme in vivo
    • Schwer B., Aronova A., Ramirez A., Braun P., Shuman S. Mammalian 2',3' cyclic nucleotide phosphodiesterase (CNP) can function as a tRNA splicing enzyme in vivo. RNA 2008, 14:204-210.
    • (2008) RNA , vol.14 , pp. 204-210
    • Schwer, B.1    Aronova, A.2    Ramirez, A.3    Braun, P.4    Shuman, S.5
  • 6
    • 38549172995 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of DR1281: a calcineurin-like phosphoesterase from Deinococcus radiodurans
    • Shin D.H., Proudfoot M., Lim H.J., Choi I.K., Yokota H., Yakunin A.F., Kim R., Kim S.H. Structural and enzymatic characterization of DR1281: a calcineurin-like phosphoesterase from Deinococcus radiodurans. Proteins 2008, 70:1000-1009.
    • (2008) Proteins , vol.70 , pp. 1000-1009
    • Shin, D.H.1    Proudfoot, M.2    Lim, H.J.3    Choi, I.K.4    Yokota, H.5    Yakunin, A.F.6    Kim, R.7    Kim, S.H.8
  • 8
    • 38349167848 scopus 로고    scopus 로고
    • Phosphodiesterase activity of CvfA is required for virulence in Staphylococcus aureus
    • Nagata M., Kaito C., Sekimizu K. Phosphodiesterase activity of CvfA is required for virulence in Staphylococcus aureus. J. Biol. Chem. 2008, 283:2176-2184.
    • (2008) J. Biol. Chem. , vol.283 , pp. 2176-2184
    • Nagata, M.1    Kaito, C.2    Sekimizu, K.3
  • 9
    • 57649171118 scopus 로고    scopus 로고
    • A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activity
    • Keppetipola N., Shuman S. A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activity. J. Biol. Chem. 2008, 283:30942-30949.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30942-30949
    • Keppetipola, N.1    Shuman, S.2
  • 10
    • 0036920683 scopus 로고    scopus 로고
    • Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily
    • Mazumder R., Iyer L.M., Vasudevan S., Aravind L. Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily. Nucleic Acids Res. 2002, 30:5229-5243.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5229-5243
    • Mazumder, R.1    Iyer, L.M.2    Vasudevan, S.3    Aravind, L.4
  • 11
    • 0344045112 scopus 로고
    • Theoretical calculations of hydrolysis energies of " high-energy" molecules. 3. Theoretical calculations on the geometric destabilization of 3',5'- and 2',3'-cyclic nucleotides
    • Marsh F.J., Weiner P., Douglas J.E., Kollman P.A., Kenyon G.L., Gerlt J.A. Theoretical calculations of hydrolysis energies of " high-energy" molecules. 3. Theoretical calculations on the geometric destabilization of 3',5'- and 2',3'-cyclic nucleotides. J. Am. Chem. Soc. 1980, 102:1660-1665.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 1660-1665
    • Marsh, F.J.1    Weiner, P.2    Douglas, J.E.3    Kollman, P.A.4    Kenyon, G.L.5    Gerlt, J.A.6
  • 12
    • 0033583733 scopus 로고    scopus 로고
    • Rapid hydrolysis of 2',3'-cAMP with a Cu(II) complex: effect of intramolecular hydrogen bonding on the basicity and reactivity of a metal-bound hydroxide
    • Wall M., Linkletter B., Williams D., Hynes R.C., Chin J. Rapid hydrolysis of 2',3'-cAMP with a Cu(II) complex: effect of intramolecular hydrogen bonding on the basicity and reactivity of a metal-bound hydroxide. J. Am. Chem. Soc. 1999, 121:4710-4711.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4710-4711
    • Wall, M.1    Linkletter, B.2    Williams, D.3    Hynes, R.C.4    Chin, J.5
  • 14
    • 34250847224 scopus 로고    scopus 로고
    • Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene
    • Miller D.J., Shuvalova L., Evdokimova E., Savchenko A., Yakunin A.F., Anderson W.F. Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene. Protein Sci. 2007, 16:1338-1348.
    • (2007) Protein Sci. , vol.16 , pp. 1338-1348
    • Miller, D.J.1    Shuvalova, L.2    Evdokimova, E.3    Savchenko, A.4    Yakunin, A.F.5    Anderson, W.F.6
  • 15
    • 73649086209 scopus 로고    scopus 로고
    • YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity
    • Rao F., See R.Y., Zhang D., Toh D.C., Ji Q., Liang Z.X. YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity. J. Biol. Chem. 2010, 285:473-482.
    • (2010) J. Biol. Chem. , vol.285 , pp. 473-482
    • Rao, F.1    See, R.Y.2    Zhang, D.3    Toh, D.C.4    Ji, Q.5    Liang, Z.X.6
  • 16
    • 67349108043 scopus 로고    scopus 로고
    • Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase
    • Rao F., Pasunooti S., Ng Y., Zhuo W., Lim L., Liu W., Liang Z.-X. Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase. Anal. Biochem. 2009, 389:138-142.
    • (2009) Anal. Biochem. , vol.389 , pp. 138-142
    • Rao, F.1    Pasunooti, S.2    Ng, Y.3    Zhuo, W.4    Lim, L.5    Liu, W.6    Liang, Z.-X.7
  • 17
    • 0031939738 scopus 로고    scopus 로고
    • A novel family of predicted phosphoesterases includes Drosophila prune protein and bacterial RecJ exonuclease
    • Aravind L., Koonin E.V. A novel family of predicted phosphoesterases includes Drosophila prune protein and bacterial RecJ exonuclease. Trends Biochem. Sci. 1998, 23:17-19.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 17-19
    • Aravind, L.1    Koonin, E.V.2
  • 18
    • 34547851775 scopus 로고    scopus 로고
    • YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity
    • Mechold U., Fang G., Ngo S., Ogryzko V., Danchin A. YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity. Nucleic Acids Res. 2007, 35:4552-4561.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4552-4561
    • Mechold, U.1    Fang, G.2    Ngo, S.3    Ogryzko, V.4    Danchin, A.5
  • 19
    • 67749113278 scopus 로고    scopus 로고
    • The functional role of a conserved loop in EAL domain-based c-di-GMP specific phosphodiesterase
    • Rao F., Qi Y., Chong H.S., Kotada M., Li B., Lescar J., Tang K., Liang Z.-X. The functional role of a conserved loop in EAL domain-based c-di-GMP specific phosphodiesterase. J. Bacteriol. 2009, 191:4722-4731.
    • (2009) J. Bacteriol. , vol.191 , pp. 4722-4731
    • Rao, F.1    Qi, Y.2    Chong, H.S.3    Kotada, M.4    Li, B.5    Lescar, J.6    Tang, K.7    Liang, Z.-X.8
  • 20
    • 47049115663 scopus 로고    scopus 로고
    • Catalytic mechanism of c-di-GMP specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa
    • Rao F., Yang Y., Qi Y., Liang Z.X. Catalytic mechanism of c-di-GMP specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa. J. Bacteriol. 2008, 190:3622-3631.
    • (2008) J. Bacteriol. , vol.190 , pp. 3622-3631
    • Rao, F.1    Yang, Y.2    Qi, Y.3    Liang, Z.X.4
  • 21
    • 0032408864 scopus 로고    scopus 로고
    • The HD domain defines a new superfamily of metal-dependent phosphohydrolases
    • Aravind L., Koonin E.V. The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Trends Biochem. Sci. 1998, 23:469-472.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 469-472
    • Aravind, L.1    Koonin, E.V.2
  • 22
    • 77949485741 scopus 로고    scopus 로고
    • Expression, purification and characterization of the acyl carrier protein phosphodiesterase from Pseudomonas aeruginosa
    • Murugan E., Kong R., Sun H., Rao F., Liang Z.X. Expression, purification and characterization of the acyl carrier protein phosphodiesterase from Pseudomonas aeruginosa. Protein Expr. Purif. 2010, 71:132-138.
    • (2010) Protein Expr. Purif. , vol.71 , pp. 132-138
    • Murugan, E.1    Kong, R.2    Sun, H.3    Rao, F.4    Liang, Z.X.5
  • 24
    • 67649295467 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase
    • Barends T.R.M., et al. Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase. Nature 2009, 459:1015-1018.
    • (2009) Nature , vol.459 , pp. 1015-1018
    • Barends, T.R.M.1
  • 25
    • 1842766260 scopus 로고    scopus 로고
    • Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response [corrected]
    • Hogg T., Mechold U., Malke H., Cashel M., Hilgenfeld R. Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response [corrected]. Cell 2004, 117:57-68.
    • (2004) Cell , vol.117 , pp. 57-68
    • Hogg, T.1    Mechold, U.2    Malke, H.3    Cashel, M.4    Hilgenfeld, R.5
  • 26
    • 33748686575 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterases: molecular regulation to clinical use
    • Bender A.T., Beavo J.A. Cyclic nucleotide phosphodiesterases: molecular regulation to clinical use. Pharmacol. Rev. 2006, 58:488-520.
    • (2006) Pharmacol. Rev. , vol.58 , pp. 488-520
    • Bender, A.T.1    Beavo, J.A.2
  • 28
    • 33745960033 scopus 로고    scopus 로고
    • Different nucleobase orientations in two cyclic 2',3'-phosphates of purine ribonucleosides: Et3NH(2',3'-cAMP) and Et3NH(2',3'-cGMP)·H2O
    • Sieroslawski K., Slepokura K., Lis T., Bogucka M., Lutomska J., Kraszewski A. Different nucleobase orientations in two cyclic 2',3'-phosphates of purine ribonucleosides: Et3NH(2',3'-cAMP) and Et3NH(2',3'-cGMP)·H2O. Acta Crystallogr. C 2006, 62:o405-o409.
    • (2006) Acta Crystallogr. C , vol.62
    • Sieroslawski, K.1    Slepokura, K.2    Lis, T.3    Bogucka, M.4    Lutomska, J.5    Kraszewski, A.6
  • 29
    • 0040115312 scopus 로고
    • Molecular and crystal structure of the free acid of cytidine 2',3' -cyclophosphate
    • Reddy B.S., Saenger W. Molecular and crystal structure of the free acid of cytidine 2',3' -cyclophosphate. Acta Crystallogr. B 1978, 34:1520-1524.
    • (1978) Acta Crystallogr. B , vol.34 , pp. 1520-1524
    • Reddy, B.S.1    Saenger, W.2
  • 31
    • 0037059780 scopus 로고    scopus 로고
    • Crystal structures of the semireduced and inhibitor-bound forms of cyclic nucleotide phosphodiesterase from Arabidopsis thaliana
    • Hofmann A., Grella M., Botos I., Filipowicz W., Wlodawer A. Crystal structures of the semireduced and inhibitor-bound forms of cyclic nucleotide phosphodiesterase from Arabidopsis thaliana. J. Biol. Chem. 2002, 277:1419-1425.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1419-1425
    • Hofmann, A.1    Grella, M.2    Botos, I.3    Filipowicz, W.4    Wlodawer, A.5
  • 32
    • 0033302071 scopus 로고    scopus 로고
    • An evolutionary classification of the metallo-beta-lactamase fold proteins
    • Aravind L. An evolutionary classification of the metallo-beta-lactamase fold proteins. In Silico Biol. 1999, 1:69-91.
    • (1999) In Silico Biol. , vol.1 , pp. 69-91
    • Aravind, L.1
  • 33
    • 34447572294 scopus 로고    scopus 로고
    • Reprogramming the tRNA-splicing activity of a bacterial RNA repair enzyme
    • Keppetipola N., Nandakumar J., Shuman S. Reprogramming the tRNA-splicing activity of a bacterial RNA repair enzyme. Nucleic Acids Res. 2007, 35:3624-3630.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3624-3630
    • Keppetipola, N.1    Nandakumar, J.2    Shuman, S.3
  • 34
    • 38049088935 scopus 로고    scopus 로고
    • Characterization of the 2',3' cyclic phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase-phosphatase and bacteriophage lambda phosphatase
    • Keppetipola N., Shuman S. Characterization of the 2',3' cyclic phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase-phosphatase and bacteriophage lambda phosphatase. Nucleic Acids Res. 2007, 35:7721-7732.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 7721-7732
    • Keppetipola, N.1    Shuman, S.2
  • 35
    • 4344646051 scopus 로고    scopus 로고
    • The HD domain of the Escherichia coli tRNA nucleotidyltransferase has 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase activities
    • Yakunin A.F., Proudfoot M., Kuznetsova E., Savchenko A., Brown G., Arrowsmith C.H., Edwards A.M. The HD domain of the Escherichia coli tRNA nucleotidyltransferase has 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase activities. J. Biol. Chem. 2004, 279:36819-36827.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36819-36827
    • Yakunin, A.F.1    Proudfoot, M.2    Kuznetsova, E.3    Savchenko, A.4    Brown, G.5    Arrowsmith, C.H.6    Edwards, A.M.7
  • 36
    • 13844276689 scopus 로고    scopus 로고
    • Crystal structure of the catalytic fragment of human brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase
    • Sakamoto Y., Tanaka N., Ichimiya T., Kurihara T., Nakamura K.T. Crystal structure of the catalytic fragment of human brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase. J. Mol. Biol. 2005, 346:789-800.
    • (2005) J. Mol. Biol. , vol.346 , pp. 789-800
    • Sakamoto, Y.1    Tanaka, N.2    Ichimiya, T.3    Kurihara, T.4    Nakamura, K.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.