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Volumn 83, Issue 1, 2005, Pages 37-45

Influence of zinc and cobalt on expression and activity of parathion hydrolase from Flavobacterium sp. ATCC27551

Author keywords

Flavobacterium; Gene regulation; Opd gene; Organophosphate degradation; Phosphotriesterase

Indexed keywords

AGROBACTERIUM; FLAVOBACTERIUM; FLAVOBACTERIUM SP.; PSEUDOMONAS; RHIZOBIUM;

EID: 23844459369     PISSN: 00483575     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pestbp.2005.03.007     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 33645268505 scopus 로고    scopus 로고
    • Drastic solutions
    • P. Bailey Drastic solutions Wellcome News 29 2001 24 25
    • (2001) Wellcome News , vol.29 , pp. 24-25
    • Bailey, P.1
  • 4
    • 0029032588 scopus 로고
    • Three-dimensional structure of the binuclear metal center of phosphotriesterase
    • M.M. Benning, J.M. Kuo, F.M. Raushel, and H.M. Holden Three-dimensional structure of the binuclear metal center of phosphotriesterase Biochemistry 34 1995 7973 7978
    • (1995) Biochemistry , vol.34 , pp. 7973-7978
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 5
    • 0017606437 scopus 로고
    • Endemic familial arthritis of Malnad-an epidemiological study
    • R.V. Bhat, and K.A. Krishnamachari Endemic familial arthritis of Malnad-an epidemiological study Indian J. Med. Res. 66 1977 777 786
    • (1977) Indian J. Med. Res. , vol.66 , pp. 777-786
    • Bhat, R.V.1    Krishnamachari, K.A.2
  • 6
    • 0032960144 scopus 로고    scopus 로고
    • NahW, a novel, inducible salicylate hydroxylase involved in mineralization of naphthalene by Pseudomonas stutzeri AN10
    • R. Bosch, E.R. Moore, E. Garcia-Valdes, and D.H. Pieper NahW, a novel, inducible salicylate hydroxylase involved in mineralization of naphthalene by Pseudomonas stutzeri AN10 J. Bacteriol. 181 1999 2315 2322
    • (1999) J. Bacteriol. , vol.181 , pp. 2315-2322
    • Bosch, R.1    Moore, E.R.2    Garcia-Valdes, E.3    Pieper, D.H.4
  • 7
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • H.W. Boyer, and D. Roulland-Dussoix A complementation analysis of the restriction and modification of DNA in Escherichia coli J. Mol. Biol. 41 1969 459 472
    • (1969) J. Mol. Biol. , vol.41 , pp. 459-472
    • Boyer, H.W.1    Roulland-Dussoix, D.2
  • 8
    • 0026073674 scopus 로고
    • Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate
    • J.J. DeFrank, and T.C. Cheng Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate J. Bacteriol. 173 1991 1938 1943
    • (1991) J. Bacteriol. , vol.173 , pp. 1938-1943
    • Defrank, J.J.1    Cheng, T.C.2
  • 9
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • D.P. Dumas, S.R. Caldwell, J.R. Wild, and F.M. Raushel Purification and properties of the phosphotriesterase from Pseudomonas diminuta J. Biol. Chem. 264 1989 19659 19665
    • (1989) J. Biol. Chem. , vol.264 , pp. 19659-19665
    • Dumas, D.P.1    Caldwell, S.R.2    Wild, J.R.3    Raushel, F.M.4
  • 10
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • D.H. Figurski, and D.R. Helinski Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans Proc. Natl. Acad. Sci. USA 73 1979 1648 1652
    • (1979) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 11
    • 0024097524 scopus 로고
    • Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp. (ATCC 27551) contain identical opd genes
    • L.L. Harper, C.S. Mcdaniel, C.E. Miller, and J.R. Wild Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp. (ATCC 27551) contain identical opd genes Appl. Environ. Microbiol. 54 1988 2586 2589
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 2586-2589
    • Harper, L.L.1    McDaniel, C.S.2    Miller, C.E.3    Wild, J.R.4
  • 12
    • 0024008341 scopus 로고
    • Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase
    • C.S. Mcdaniel, L.L. Harper, and J.R. Wild Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase J. Bacteriol. 170 1988 2306 2311
    • (1988) J. Bacteriol. , vol.170 , pp. 2306-2311
    • McDaniel, C.S.1    Harper, L.L.2    Wild, J.R.3
  • 14
    • 0024332036 scopus 로고
    • Parathion hydrolase specified by the Flavobacterium opd gene-relationship between the gene and protein
    • W.W. Mulbry, and J.S. Karns Parathion hydrolase specified by the Flavobacterium opd gene-relationship between the gene and protein J. Bacteriol. 171 1989 6740 6746
    • (1989) J. Bacteriol. , vol.171 , pp. 6740-6746
    • Mulbry, W.W.1    Karns, J.S.2
  • 15
    • 0024501620 scopus 로고
    • Purification and characterization of three parathion hydrolases from Gram-negative bacterial strains
    • W.W. Mulbry, and J.S. Karns Purification and characterization of three parathion hydrolases from Gram-negative bacterial strains Appl. Environ. Microbiol. 55 1989 289 293
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 289-293
    • Mulbry, W.W.1    Karns, J.S.2
  • 16
    • 0022479569 scopus 로고
    • Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by southern hybridization with opd from Pseudomonas diminuta
    • W.W. Mulbry, J.S. Karns, P.C. Kearney, J.O. Nelson, C.S. Mcdaniel, and J.R. Wild Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by southern hybridization with opd from Pseudomonas diminuta Appl. Environ. Microbiol. 51 1986 926 930
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 926-930
    • Mulbry, W.W.1    Karns, J.S.2    Kearney, P.C.3    Nelson, J.O.4    McDaniel, C.S.5    Wild, J.R.6
  • 17
    • 0041778578 scopus 로고
    • Physical comparison of parathion hydrolase plasmids from Pseudomonas diminuta and Flavobacterium sp.
    • W.W. Mulbry, P.C. Kearney, J.O. Nelson, and J.S. Karns Physical comparison of parathion hydrolase plasmids from Pseudomonas diminuta and Flavobacterium sp. Plasmid 18 1987 173 177
    • (1987) Plasmid , vol.18 , pp. 173-177
    • Mulbry, W.W.1    Kearney, P.C.2    Nelson, J.O.3    Karns, J.S.4
  • 18
    • 0018330872 scopus 로고
    • Chemical, physical, and biological methods for the disposal and detoxification of pesticides
    • D.M. Munnecke Chemical, physical, and biological methods for the disposal and detoxification of pesticides Residue Rev. 70 1979 1 26
    • (1979) Residue Rev. , vol.70 , pp. 1-26
    • Munnecke, D.M.1
  • 19
    • 0026748791 scopus 로고
    • Characterization of the zinc binding site of bacterial phosphotriesterase
    • G.A. Omburo, J.M. Kuo, L.S. Mullins, and F.M. Raushel Characterization of the zinc binding site of bacterial phosphotriesterase J. Biol. Chem. 267 1992 13278 13283
    • (1992) J. Biol. Chem. , vol.267 , pp. 13278-13283
    • Omburo, G.A.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 20
    • 0031745849 scopus 로고    scopus 로고
    • Towards a biocatalyst for (S)-styrene oxide production: Characterization of the styrene degradation pathway of Pseudomonas sp. strain VLB120
    • S. Panke, B. Witholt, A. Schmid, and M.G. Wubbolts Towards a biocatalyst for (S)-styrene oxide production: characterization of the styrene degradation pathway of Pseudomonas sp. strain VLB120 Appl. Environ. Microbiol. 64 1998 2032 2043
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2032-2043
    • Panke, S.1    Witholt, B.2    Schmid, A.3    Wubbolts, M.G.4
  • 21
    • 0025968498 scopus 로고
    • Purification and characterization of a secreted recombinant phosphotriesterase (parathion hydrolase) from Streptomyces lividans
    • S.S. Rowland, M.K. Speedie, and B.M. Pogell Purification and characterization of a secreted recombinant phosphotriesterase (parathion hydrolase) from Streptomyces lividans Appl. Environ. Microbiol. 57 1991 440 444
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 440-444
    • Rowland, S.S.1    Speedie, M.K.2    Pogell, B.M.3
  • 22
    • 0020699917 scopus 로고
    • Cloning and expression in Escherichia coli of the naphthalene degradation genes from plasmid NAH7
    • M.A. Schell Cloning and expression in Escherichia coli of the naphthalene degradation genes from plasmid NAH7 J. Bacteriol. 153 1983 822 829
    • (1983) J. Bacteriol. , vol.153 , pp. 822-829
    • Schell, M.A.1
  • 23
    • 0030027260 scopus 로고    scopus 로고
    • Comparative genome mapping of Pseudomonas aeruginosa PAO with P. aeruginosa C, which belongs to a major clone in cystic fibrosis patients and aquatic habitats
    • K.D. Schmidt, B. Tummler, and U. Romling Comparative genome mapping of Pseudomonas aeruginosa PAO with P. aeruginosa C, which belongs to a major clone in cystic fibrosis patients and aquatic habitats J. Bacteriol. 178 1996 85 93
    • (1996) J. Bacteriol. , vol.178 , pp. 85-93
    • Schmidt, K.D.1    Tummler, B.2    Romling, U.3
  • 25
    • 0024444644 scopus 로고
    • Parathion hydrolase gene from Pseudomonas diminuta MG: Subcloning, complete nucleotide-sequence, and expression of the mature portion of the enzyme in Escherichia coli
    • C.M. Serdar, D.C. Murdock, and M.F. Rohde Parathion hydrolase gene from Pseudomonas diminuta MG: subcloning, complete nucleotide-sequence, and expression of the mature portion of the enzyme in Escherichia coli Bio-Technology 7 1989 1151 1155
    • (1989) Bio-Technology , vol.7 , pp. 1151-1155
    • Serdar, C.M.1    Murdock, D.C.2    Rohde, M.F.3
  • 26
    • 0015891473 scopus 로고
    • A Flavobacterium sp. that degrades diazinon and parathion
    • N. Sethunathan, and T. Yoshida A Flavobacterium sp. that degrades diazinon and parathion Can. J. Microbiol. 19 1973 873 875
    • (1973) Can. J. Microbiol. , vol.19 , pp. 873-875
    • Sethunathan, N.1    Yoshida, T.2
  • 27
    • 0038559866 scopus 로고    scopus 로고
    • Transposon-like organization of the plasmid-borne organophosphate degradation (opd) gene cluster found in Flavobacterium sp.
    • D. Siddavattam, S. Khajamohiddin, B. Manavathi, S.B. Pakala, and M.J. Merrick Transposon-like organization of the plasmid-borne organophosphate degradation (opd) gene cluster found in Flavobacterium sp. Appl. Environ. Microbiol. 69 2003 2533 2539
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2533-2539
    • Siddavattam, D.1    Khajamohiddin, S.2    Manavathi, B.3    Pakala, S.B.4    Merrick, M.J.5
  • 28
    • 0036069930 scopus 로고    scopus 로고
    • Localisation of identical organophosphorus degrading (opd) genes on genetically dissimilar indigenous plasmids of soil bacteria: PCR amplification, cloning and sequencing of the opd gene from Flavobacterium balustinum
    • S. Somara, B. Manavathi, C. Tebbe, and D. Siddavattam Localisation of identical organophosphorus degrading (opd) genes on genetically dissimilar indigenous plasmids of soil bacteria: PCR amplification, cloning and sequencing of the opd gene from Flavobacterium balustinum Indian J. Exp. Biol. 40 2002 774 779
    • (2002) Indian J. Exp. Biol. , vol.40 , pp. 774-779
    • Somara, S.1    Manavathi, B.2    Tebbe, C.3    Siddavattam, D.4
  • 29
    • 0042171741 scopus 로고    scopus 로고
    • Over-expression of parathion hydrolase of Flavobacterium balustinum in E. coli: Purification and characterisation of His-tagged parathion hydrolase
    • S. Somara, B. Manavathi, C. Tebbe, and D. Siddavattam Over-expression of parathion hydrolase of Flavobacterium balustinum in E. coli: purification and characterisation of His-tagged parathion hydrolase Indian J. Biochem. Biophys. 39 2002 82 86
    • (2002) Indian J. Biochem. Biophys. , vol.39 , pp. 82-86
    • Somara, S.1    Manavathi, B.2    Tebbe, C.3    Siddavattam, D.4
  • 30
    • 0029551095 scopus 로고
    • Plasmid mediated organophosphate pesticide degradation by Flavobacterium balustinum
    • S. Somara, and D. Siddavattam Plasmid mediated organophosphate pesticide degradation by Flavobacterium balustinum Biochem. Mol. Biol. Int. 36 1995 627 631
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 627-631
    • Somara, S.1    Siddavattam, D.2
  • 32
    • 0024552237 scopus 로고
    • A gene coding for a membrane-bound hydrolase is expressed as a secreted, soluble enzyme in Streptomyces lividans
    • J.G. Steiert, B.M. Pogell, M.K. Speedie, and J. Laredo A gene coding for a membrane-bound hydrolase is expressed as a secreted, soluble enzyme in Streptomyces lividans Biotechnol 7 1989 65 68
    • (1989) Biotechnol , vol.7 , pp. 65-68
    • Steiert, J.G.1    Pogell, B.M.2    Speedie, M.K.3    Laredo, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.