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Volumn 18, Issue 1, 1997, Pages 49-55

Nucleotide sequence of a gene encoding an organophosphorus nerve agent degrading enzyme from Alteromonas haloplanktis

Author keywords

Alteromonas organophosphorus acid anhydrolase gene; Sequencing and functional homology to prolidase; X Pro dipeptidase

Indexed keywords

CHOLINESTERASE INHIBITOR; DIPEPTIDASE; DIPEPTIDE; HYDROLASE; ORGANOPHOSPHORUS COMPOUND; PESTICIDE; PROLINE DIPEPTIDASE;

EID: 0030901409     PISSN: 13675435     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.jim.2900358     Document Type: Article
Times cited : (74)

References (29)
  • 1
    • 0023701385 scopus 로고
    • Initial characterization of the organophosphate acid anhydrolase activity in the clam, Rangia cuneata
    • Anderson RS, HD Durst and WG Landis. 1988. Initial characterization of the organophosphate acid anhydrolase activity in the clam, Rangia cuneata. Comp Biochem Physiol 91C: 575-578.
    • (1988) Comp Biochem Physiol , vol.91 C , pp. 575-578
    • Anderson, R.S.1    Durst, H.D.2    Landis, W.G.3
  • 3
    • 0002135589 scopus 로고
    • Gene cloning and expression
    • (Gerhardt P, RGE Murray, WA Wood and NR Krieg, eds), American Society for Microbiology, Washington, DC
    • Bagdasarian M and MM Bagdasarian. 1994. Gene cloning and expression. In: Methods for General and Molecular Bacteriology (Gerhardt P, RGE Murray, WA Wood and NR Krieg, eds), pp 409-412, American Society for Microbiology, Washington, DC.
    • (1994) Methods for General and Molecular Bacteriology , pp. 409-412
    • Bagdasarian, M.1    Bagdasarian, M.M.2
  • 4
    • 0027292250 scopus 로고
    • Purification and properties of a highly active organophosphorus acid anhydrolase from Alteromonas undina
    • Cheng T-c, SP Harvey and AN Stroup. 1993. Purification and properties of a highly active organophosphorus acid anhydrolase from Alteromonas undina. Appl Environ Microbiol 59: 3138-3140.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 3138-3140
    • Cheng, T.-C.1    Harvey, S.P.2    Stroup, A.N.3
  • 5
    • 0029928952 scopus 로고    scopus 로고
    • Cloning, expression, and nucleotide sequence of a bacterial enzyme for decontamination of organophosphorus nerve agents
    • Cheng T-c, SP Harvey and GL Chen. 1996. Cloning, expression, and nucleotide sequence of a bacterial enzyme for decontamination of organophosphorus nerve agents. Appl Environ Microbiol 62: 1636-1641.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1636-1641
    • Cheng, T.-C.1    Harvey, S.P.2    Chen, G.L.3
  • 6
    • 0030175926 scopus 로고    scopus 로고
    • A cloned bacterial enzyme for nerve agent decontamination
    • Cheng T-C, and JJ Calomiris. 1996. A cloned bacterial enzyme for nerve agent decontamination. Enz Microbial Tech 18: 597-601.
    • (1996) Enz Microbial Tech , vol.18 , pp. 597-601
    • Cheng, T.-C.1    Calomiris, J.J.2
  • 7
    • 0026073674 scopus 로고
    • Purification and properties of an organophosphorus acid anhydrolase from a halophilic bacterial isolate
    • DeFrank JJ and T-C Cheng. 1991. Purification and properties of an organophosphorus acid anhydrolase from a halophilic bacterial isolate. J Bacteriol 173: 1938-1943.
    • (1991) J Bacteriol , vol.173 , pp. 1938-1943
    • DeFrank, J.J.1    Cheng, T.-C.2
  • 9
    • 0019809411 scopus 로고
    • Modified colorimetric ninhydrin methods for peptidase assay
    • Doi E, D Shibata and T Matoba. 1981. Modified colorimetric ninhydrin methods for peptidase assay. Anal Biochem 118: 173-184.
    • (1981) Anal Biochem , vol.118 , pp. 173-184
    • Doi, E.1    Shibata, D.2    Matoba, T.3
  • 10
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas DP, SR Caldwell, JR Wild and FR Raushel. 1989. Purification and properties of the phosphotriesterase from Pseudomonas diminuta. J Biol Chem 264: 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.R.4
  • 11
    • 0025117439 scopus 로고
    • Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta
    • Dumas DP, HD Durst, WG Landis, FM Raushel and JR Wild. 1990. Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta. Arch Biochem Biophys 277: 155-159.
    • (1990) Arch Biochem Biophys , vol.277 , pp. 155-159
    • Dumas, D.P.1    Durst, H.D.2    Landis, W.G.3    Raushel, F.M.4    Wild, J.R.5
  • 12
    • 0020034142 scopus 로고
    • Human erythrocyte prolidase and prolidase deficiency
    • Endo F, I Matsuda, S Tanaka and A Ogata. 1982. Human erythrocyte prolidase and prolidase deficiency. Pediatric Res 16: 227-231.
    • (1982) Pediatric Res , vol.16 , pp. 227-231
    • Endo, F.1    Matsuda, I.2    Tanaka, S.3    Ogata, A.4
  • 13
    • 0023552985 scopus 로고
    • Immunochemical studies of human prolidase with monoclonal and polyclonal antibodies: Absence of the subunit of prolidase in erythrocytes from a patient with prolidase deficiency
    • Endo F, K Motohara, Y Indo and I Matsuda. 1987. Immunochemical studies of human prolidase with monoclonal and polyclonal antibodies: absence of the subunit of prolidase in erythrocytes from a patient with prolidase deficiency. Pediatric Res 22: 627-633.
    • (1987) Pediatric Res , vol.22 , pp. 627-633
    • Endo, F.1    Motohara, K.2    Indo, Y.3    Matsuda, I.4
  • 15
    • 0020645065 scopus 로고
    • Uses of the transposon γδ in the analysis of cloned genes
    • Guyer MS. 1983. Uses of the transposon γδ in the analysis of cloned genes. Meth Enzymol 101: 362-369.
    • (1983) Meth Enzymol , vol.101 , pp. 362-369
    • Guyer, M.S.1
  • 16
    • 0006724944 scopus 로고
    • Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp (ATCC 27551) contain identical opd genes
    • Harper LL, CS McDaniel, CE Miller and JR Wild. 1988. Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp (ATCC 27551) contain identical opd genes. Appl Environ Microbiol 44: 246-249.
    • (1988) Appl Environ Microbiol , vol.44 , pp. 246-249
    • Harper, L.L.1    McDaniel, C.S.2    Miller, C.E.3    Wild, J.R.4
  • 17
    • 0020037124 scopus 로고
    • Hydrolysis of nerve gas by squid type diisopropylphosphorofluoridate hydrolyzing enzyme on agarose resin
    • Hoskin FC and AH Rousch. 1982. Hydrolysis of nerve gas by squid type diisopropylphosphorofluoridate hydrolyzing enzyme on agarose resin. Science 215: 1255-1257.
    • (1982) Science , vol.215 , pp. 1255-1257
    • Hoskin, F.C.1    Rousch, A.H.2
  • 18
    • 0024075233 scopus 로고
    • Sequencing of proteins from two-dimentional gels by using in situ digestion and transfer of peptides to polyvinylidene difluoride membranes: Application to proteins associated with sensitization in Aplysia
    • Kennedy TE, MA Gawinowicz, A Barzilai, ER Kandel and JD Sweatt. 1988. Sequencing of proteins from two-dimentional gels by using in situ digestion and transfer of peptides to polyvinylidene difluoride membranes: application to proteins associated with sensitization in Aplysia. Proc Natl Acad Sci 85: 7008-1012.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 7008-11012
    • Kennedy, T.E.1    Gawinowicz, M.A.2    Barzilai, A.3    Kandel, E.R.4    Sweatt, J.D.5
  • 19
    • 0023277824 scopus 로고
    • Discovery of multiple organofluorophosphate hydrolyzing activities in the protozoan Tetrahymena thermophila
    • Landis WG, HD Durst, RE Savage Jr, DM Haley, MV Haley and DW Johnson. 1987. Discovery of multiple organofluorophosphate hydrolyzing activities in the protozoan Tetrahymena thermophila. J Appl Toxicol 7: 35-41.
    • (1987) J Appl Toxicol , vol.7 , pp. 35-41
    • Landis, W.G.1    Durst, H.D.2    Savage Jr., R.E.3    Haley, D.M.4    Haley, M.V.5    Johnson, D.W.6
  • 20
    • 0342440991 scopus 로고
    • Partial characterization of a rat liver enzyme that hydrolyzes sarin, soman, tabun and DFP
    • Little JS, CA Broomfield, LJ Boucher and MK Fox-Talbot. 1986. Partial characterization of a rat liver enzyme that hydrolyzes sarin, soman, tabun and DFP. Fed Proc 45: 791.
    • (1986) Fed Proc , vol.45 , pp. 791
    • Little, J.S.1    Broomfield, C.A.2    Boucher, L.J.3    Fox-Talbot, M.K.4
  • 21
    • 0023665369 scopus 로고
    • Rapid sequencing of cloned DNA using a transposon for bidirectional priming: Sequence of the Escherichia coli K-12 avtA gene
    • Liu L, W Whalen, A Das and CM Berg. 1987. Rapid sequencing of cloned DNA using a transposon for bidirectional priming: sequence of the Escherichia coli K-12 avtA gene. Nucleic Acid Res 15: 9461-9469.
    • (1987) Nucleic Acid Res , vol.15 , pp. 9461-9469
    • Liu, L.1    Whalen, W.2    Das, A.3    Berg, C.M.4
  • 22
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudira P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262: 10035-10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudira, P.1
  • 23
    • 84872639802 scopus 로고
    • An enzyme in animal tissue capable of hydrolyzing the phosphorus fluorine bond of alkyl fluorophosphates
    • Mazur A. 1946. An enzyme in animal tissue capable of hydrolyzing the phosphorus fluorine bond of alkyl fluorophosphates. J Biol Chem 164: 271-289.
    • (1946) J Biol Chem , vol.164 , pp. 271-289
    • Mazur, A.1
  • 24
    • 0028894628 scopus 로고
    • Purification and characterization of a dipeptidase from Lactobacillus sake
    • Montel MC, MP Seronie, R Talon and M Hebraud. 1995. Purification and characterization of a dipeptidase from Lactobacillus sake. Appl Environ Microbiol 61: 837-839.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 837-839
    • Montel, M.C.1    Seronie, M.P.2    Talon, R.3    Hebraud, M.4
  • 25
    • 0024332036 scopus 로고
    • Parathion hydrolase specified by the Flavobacterium opd gene: Relationship between the gene and protein
    • Mulbry W and J Karns. 1989. Parathion hydrolase specified by the Flavobacterium opd gene: relationship between the gene and protein. J Bacteriol 171: 6740-6746.
    • (1989) J Bacteriol , vol.171 , pp. 6740-6746
    • Mulbry, W.1    Karns, J.2
  • 26
    • 0025001827 scopus 로고
    • Nucleotide sequence between the fadB gene and rrnA operon from Escherichia coli
    • Nakahigashi K and H Inokuchi. 1990. Nucleotide sequence between the fadB gene and rrnA operon from Escherichia coli. Nucleic Acids Res 18: 6439.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6439
    • Nakahigashi, K.1    Inokuchi, H.2
  • 27
    • 0000488319 scopus 로고
    • Disorders of proline and hydroxyproline metabolism
    • (Scriver RC, AL Beaudet, WS Sly and D Valle, eds), 7th edn, McGraw-Hill, New York
    • Phang JM, GC Yeh and CR Scnver. 1995. Disorders of proline and hydroxyproline metabolism. In: The Metabolic and Molecular Bases of Inherited Disease (Scriver RC, AL Beaudet, WS Sly and D Valle, eds), 7th edn, pp 1125-1146, McGraw-Hill, New York.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 1125-1146
    • Phang, J.M.1    Yeh, G.C.2    Scnver, C.R.3
  • 29
    • 0016668768 scopus 로고
    • Organophosphate-detoxicating enzymes in E. coli: Gel filtration and isoelectric focusing of DFPase, paraoxonase and unspecific phosphohydrolases
    • Zech R and KD Wigand. 1975. Organophosphate-detoxicating enzymes in E. coli: gel filtration and isoelectric focusing of DFPase, paraoxonase and unspecific phosphohydrolases. Experientia 15: 157-158.
    • (1975) Experientia , vol.15 , pp. 157-158
    • Zech, R.1    Wigand, K.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.