메뉴 건너뛰기




Volumn 583, Issue 2, 2009, Pages 443-448

Enzymatic characteristics of two novel Myxococcus xanthus enzymes, PdeA and PdeB, displaying 3′,5′- and 2′,3′-cAMP phosphodiesterase, and phosphatase activities

Author keywords

cAMP phosphodiesterase; Myxococcus xanthus; Phosphatase

Indexed keywords

2',3' CYCLIC NUCLEOTIDE 3' PHOSPHODIESTERASE; ADENOSINE; ADENOSINE 2',3' PHOSPHATE; BACTERIAL ENZYME; COBALT; CYCLIC AMP PHOSPHODIESTERASE; MANGANESE; NUCLEOTIDASE; PHOSPHATASE; PROTEIN PDEA; PROTEIN PDEB; UNCLASSIFIED DRUG;

EID: 58149512841     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.12.044     Document Type: Article
Times cited : (16)

References (29)
  • 2
    • 0031820874 scopus 로고    scopus 로고
    • Catalytic mechanism and regulation of mammalian adenylyl cyclases
    • Tang W.J., and Hurley J.H. Catalytic mechanism and regulation of mammalian adenylyl cyclases. Mol. Pharmacol. 54 (1998) 231-240
    • (1998) Mol. Pharmacol. , vol.54 , pp. 231-240
    • Tang, W.J.1    Hurley, J.H.2
  • 3
    • 0242352429 scopus 로고    scopus 로고
    • Cell behavior and cell-cell communication during fruiting body morphogenesis in Myxococcus xanthus
    • Jelsbak L., and Søgaard-Andersen L. Cell behavior and cell-cell communication during fruiting body morphogenesis in Myxococcus xanthus. J. Microbiol. Meth. 55 (2003) 829-839
    • (2003) J. Microbiol. Meth. , vol.55 , pp. 829-839
    • Jelsbak, L.1    Søgaard-Andersen, L.2
  • 4
    • 3042548915 scopus 로고    scopus 로고
    • Signaling in Myxobacteria
    • Kaiser D. Signaling in Myxobacteria. Annu. Rev. Microbiol. 58 (2004) 75-98
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 75-98
    • Kaiser, D.1
  • 5
    • 0018869606 scopus 로고
    • Sequential changes in the cyclic nucleotide levels and cyclic phosphodiesterase activities during development of M. Xanthus
    • Ho J., and McCurdy H.D. Sequential changes in the cyclic nucleotide levels and cyclic phosphodiesterase activities during development of M. Xanthus. Curr. Microbiol. 3 (1980) 197-202
    • (1980) Curr. Microbiol. , vol.3 , pp. 197-202
    • Ho, J.1    McCurdy, H.D.2
  • 6
    • 0017801635 scopus 로고
    • Changes in cyclic AMP levels during development in Myxococcus xanthus
    • Yajko D.M., and Zusman D.R. Changes in cyclic AMP levels during development in Myxococcus xanthus. J. Bacteriol. 133 (1978) 1540-1542
    • (1978) J. Bacteriol. , vol.133 , pp. 1540-1542
    • Yajko, D.M.1    Zusman, D.R.2
  • 7
    • 0036283445 scopus 로고    scopus 로고
    • An adenylyl cyclase, CyaA, of Myxococcus xanthus functions in signal transduction during osmotic stress
    • Kimura Y., Mishima Y., Nakano H., and Takegawa K. An adenylyl cyclase, CyaA, of Myxococcus xanthus functions in signal transduction during osmotic stress. J. Bacteriol. 184 (2002) 3578-3585
    • (2002) J. Bacteriol. , vol.184 , pp. 3578-3585
    • Kimura, Y.1    Mishima, Y.2    Nakano, H.3    Takegawa, K.4
  • 8
    • 18244395068 scopus 로고    scopus 로고
    • An adenylyl cyclase, CyaB, acts as an osmosensor in Myxococcus xanthus
    • Kimura Y., Ohtani M., and Takegawa K. An adenylyl cyclase, CyaB, acts as an osmosensor in Myxococcus xanthus. J. Bacteriol. 187 (2005) 3593-3598
    • (2005) J. Bacteriol. , vol.187 , pp. 3593-3598
    • Kimura, Y.1    Ohtani, M.2    Takegawa, K.3
  • 9
    • 0037083671 scopus 로고    scopus 로고
    • 3′,5′-cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism
    • Richter W. 3′,5′-cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism. Proteins 46 (2002) 278-286
    • (2002) Proteins , vol.46 , pp. 278-286
    • Richter, W.1
  • 10
    • 0029815090 scopus 로고    scopus 로고
    • Identification of the cpdA gene encoding cyclic 3′,5′-adenosine monophosphate phosphodiesterase in Escherichia coli
    • Imamura R., Yamanaka K., Ogura T., Hiraga S., Fujita N., Ishihama A., and Niki H. Identification of the cpdA gene encoding cyclic 3′,5′-adenosine monophosphate phosphodiesterase in Escherichia coli. J. Biol. Chem. 271 (1996) 25423-25429
    • (1996) J. Biol. Chem. , vol.271 , pp. 25423-25429
    • Imamura, R.1    Yamanaka, K.2    Ogura, T.3    Hiraga, S.4    Fujita, N.5    Ishihama, A.6    Niki, H.7
  • 11
    • 30744467201 scopus 로고    scopus 로고
    • Contribution of cyclic nucleotide phosphodiesterases, PdeA and PdeB, in adaptation of Myxococcus xanthus cells to osmotic or high temperature stress
    • Kimura Y., Nakatuma H., Sato N., and Ohtani M. Contribution of cyclic nucleotide phosphodiesterases, PdeA and PdeB, in adaptation of Myxococcus xanthus cells to osmotic or high temperature stress. J. Bacteriol. 188 (2006) 823-828
    • (2006) J. Bacteriol. , vol.188 , pp. 823-828
    • Kimura, Y.1    Nakatuma, H.2    Sato, N.3    Ohtani, M.4
  • 12
    • 28544433399 scopus 로고    scopus 로고
    • The Rv0805 gene from Mycobacterium tuberculosis encodes a 3′,5′-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis
    • Shenoy A.R., Sreenath N., Podobnik M., Kovačevič M., and Visweswariah S.S. The Rv0805 gene from Mycobacterium tuberculosis encodes a 3′,5′-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis. Biochemistry 44 (2005) 15695-15704
    • (2005) Biochemistry , vol.44 , pp. 15695-15704
    • Shenoy, A.R.1    Sreenath, N.2    Podobnik, M.3    Kovačevič, M.4    Visweswariah, S.S.5
  • 13
    • 0009508940 scopus 로고
    • A study of the substrate specificity and other properties of the alkaline phosphatase of Escherichia coli
    • Heppel L.A., Harkness D.R., and Hilmoe R.J. A study of the substrate specificity and other properties of the alkaline phosphatase of Escherichia coli. J. Biol. Chem. 237 (1962) 841-846
    • (1962) J. Biol. Chem. , vol.237 , pp. 841-846
    • Heppel, L.A.1    Harkness, D.R.2    Hilmoe, R.J.3
  • 14
    • 34047250594 scopus 로고    scopus 로고
    • Ecto-5′-nucleotidase: structure function relationships
    • Sträter N. Ecto-5′-nucleotidase: structure function relationships. Purinergic 2 (2006) 343-350
    • (2006) Purinergic , vol.2 , pp. 343-350
    • Sträter, N.1
  • 15
    • 0026729643 scopus 로고
    • 5′-nucleotidase:molecular structure and functional aspects
    • Zimmermann H. 5′-nucleotidase:molecular structure and functional aspects. Biochem. J. 285 (1992) 345-365
    • (1992) Biochem. J. , vol.285 , pp. 345-365
    • Zimmermann, H.1
  • 16
    • 0001432327 scopus 로고
    • A new cyclic phosphodiesterase having a 3′-nucleotidase activity from Escherichia coli B.
    • Anraku Y. A new cyclic phosphodiesterase having a 3′-nucleotidase activity from Escherichia coli B. J. Biol. Chem. 239 (1964) 3412-3419
    • (1964) J. Biol. Chem. , vol.239 , pp. 3412-3419
    • Anraku, Y.1
  • 17
    • 0014459066 scopus 로고
    • Cyclic phosphodiesterase having 3′-nucleotidase activity from Bacillus subtilis
    • Shimada K., and Sugino Y. Cyclic phosphodiesterase having 3′-nucleotidase activity from Bacillus subtilis. Biochim. Biophys. Acta 185 (1969) 367-380
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 367-380
    • Shimada, K.1    Sugino, Y.2
  • 18
    • 0014408253 scopus 로고
    • A cyclic phosphodiesterase with 3′-nucleotidase activity from Proteus mirabilis
    • Center M.S., and Behal F.J. A cyclic phosphodiesterase with 3′-nucleotidase activity from Proteus mirabilis. J. Biol. Chem. 243 (1968) 138-143
    • (1968) J. Biol. Chem. , vol.243 , pp. 138-143
    • Center, M.S.1    Behal, F.J.2
  • 19
    • 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., and 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. 279 (2004) 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
  • 20
    • 0014198967 scopus 로고
    • The 5′-nucleotidase of Escherichia coli
    • Neu H.C. The 5′-nucleotidase of Escherichia coli. J. Biol. Chem. 242 (1967) 3896-3904
    • (1967) J. Biol. Chem. , vol.242 , pp. 3896-3904
    • Neu, H.C.1
  • 21
    • 0027433612 scopus 로고
    • UDP-sugar hydrolase isozymes in Salmonella enterica and Escherichia coli: silent alleles of ushA in related strains of group I Salmonella isolates, and of ushB in wild-type and K12 strains of E. Coli, indicate recent and early silencing events, respectively
    • Edwards C.J., Innes D.J., Burns D.M., and Beacham I.R. UDP-sugar hydrolase isozymes in Salmonella enterica and Escherichia coli: silent alleles of ushA in related strains of group I Salmonella isolates, and of ushB in wild-type and K12 strains of E. Coli, indicate recent and early silencing events, respectively. FEMS Microbiol. Lett. 114 (1993) 293-298
    • (1993) FEMS Microbiol. Lett. , vol.114 , pp. 293-298
    • Edwards, C.J.1    Innes, D.J.2    Burns, D.M.3    Beacham, I.R.4
  • 22
    • 11144227620 scopus 로고    scopus 로고
    • General enzymatic screens identify three new nucleotidases in Escherichia coli Biochemical characterization of SurE, YfbR, and YjjG
    • Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., and Yakunin A.F. General enzymatic screens identify three new nucleotidases in Escherichia coli Biochemical characterization of SurE, YfbR, and YjjG. J. Biol. Chem. 279 (2004) 54687-54694
    • (2004) J. Biol. Chem. , vol.279 , pp. 54687-54694
    • Proudfoot, M.1    Kuznetsova, E.2    Brown, G.3    Rao, N.N.4    Kitagawa, M.5    Mori, H.6    Savchenko, A.7    Yakunin, A.F.8
  • 23
    • 0035873714 scopus 로고    scopus 로고
    • Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase
    • O'Brien P.J., and Herschlag D. Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase. Biochemistry 40 (2001) 5691-5699
    • (2001) Biochemistry , vol.40 , pp. 5691-5699
    • O'Brien, P.J.1    Herschlag, D.2
  • 24
    • 0027991788 scopus 로고
    • Phosphodiesterase activity is a novel property of alkaline phosphatase from osseous plate
    • Rezende A.A., Pizauro J.M., Ciancaglini P., and Leone F.A. Phosphodiesterase activity is a novel property of alkaline phosphatase from osseous plate. Biochem. J. 301 (1994) 517-522
    • (1994) Biochem. J. , vol.301 , pp. 517-522
    • Rezende, A.A.1    Pizauro, J.M.2    Ciancaglini, P.3    Leone, F.A.4
  • 25
    • 0019451178 scopus 로고
    • Characterization of 3′,5′-cyclic AMP phosphodiesterase in Klebsiella aerogenes and its role in substrate-accelerated death
    • Calcott P.H., and Calvert T.J. Characterization of 3′,5′-cyclic AMP phosphodiesterase in Klebsiella aerogenes and its role in substrate-accelerated death. J. Gen. Microbiol. 122 (1981) 313-321
    • (1981) J. Gen. Microbiol. , vol.122 , pp. 313-321
    • Calcott, P.H.1    Calvert, T.J.2
  • 26
    • 0014945470 scopus 로고
    • Cyclic 3′,5′-nucleotide phosphodiesterase of Serratia marcescens
    • Okabayashi T., and Ide M. Cyclic 3′,5′-nucleotide phosphodiesterase of Serratia marcescens. Biochim. Biophys. Acta 220 (1970) 116-123
    • (1970) Biochim. Biophys. Acta , vol.220 , pp. 116-123
    • Okabayashi, T.1    Ide, M.2
  • 28
    • 0031721648 scopus 로고    scopus 로고
    • A 3′,5′ cyclic AMP (cAMP) phosphodiesterase modulates cAMP levels and optimizes competence in Haemophilus influenzae Rd
    • Macfadyen L.P., Ma C., and Redfield R.J. A 3′,5′ cyclic AMP (cAMP) phosphodiesterase modulates cAMP levels and optimizes competence in Haemophilus influenzae Rd. J. Bacteriol. 180 (1998) 4401-4405
    • (1998) J. Bacteriol. , vol.180 , pp. 4401-4405
    • Macfadyen, L.P.1    Ma, C.2    Redfield, R.J.3
  • 29
    • 0036230974 scopus 로고    scopus 로고
    • Intracellular cyclic AMP concentration is decreased in Salmonella typhimurium fur mutants
    • Campoy S., Jara M., Busquets N., de Rozas A.M., Badiola I., and Barbé J. Intracellular cyclic AMP concentration is decreased in Salmonella typhimurium fur mutants. Microbiology 148 (2002) 1039-1048
    • (2002) Microbiology , vol.148 , pp. 1039-1048
    • Campoy, S.1    Jara, M.2    Busquets, N.3    de Rozas, A.M.4    Badiola, I.5    Barbé, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.