메뉴 건너뛰기




Volumn 62, Issue 5, 1996, Pages 1636-1641

Cloning and expression of a gene encoding a bacterial enzyme for decontamination of organophosphorus nerve agents and nucleotide sequence of the enzyme

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE P; CHOLINESTERASE INHIBITOR; ORGANOPHOSPHORUS COMPOUND; PESTICIDE; PROLINE DIPEPTIDASE; SARIN; SOMAN;

EID: 0029928952     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.62.5.1636-1641.1996     Document Type: Article
Times cited : (125)

References (32)
  • 3
    • 0027292250 scopus 로고
    • Purification and properties of a highly active organophosphorus acid anhydrolase from Alteromonas undina
    • Cheng, T.-C., S. P. Harvey, and A. N. 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
  • 4
    • 15844373906 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y
    • Crombrugghe, B., and I. Pastan. 1978. The operon. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1978) The Operon
    • Crombrugghe, B.1    Pastan, I.2
  • 7
    • 0026073674 scopus 로고
    • Purification and properties of an organophosphorus acid anhydrolase from a halophilic bacterial isolate
    • DeFrank, J. J., and T.-C. Cheng. 1191. Purification and properties of an organophosphorus acid anhydrolase from a halophilic bacterial isolate. J. Bacteriol. 173:1938-1943.
    • (1191) J. Bacteriol. , vol.173 , pp. 1938-1943
    • DeFrank, J.J.1    Cheng, T.-C.2
  • 8
    • 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
  • 9
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D. P., S. R. Caldwell, J. R. Wild, and F. R. 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
  • 10
    • 0025117439 scopus 로고
    • Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D. P., H. D. Durst, W. G. Landis, F. M. Raushel, and J. R. 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
  • 11
    • 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. Pediatr. Res. 16:227-231.
    • (1982) Pediatr. Res. , vol.16 , pp. 227-231
    • Endo, F.1    Matsuda, I.2    Tanaka, S.3    Ogata, A.4
  • 12
    • 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. Pediatr. Res. 22:627-633.
    • (1987) Pediatr. Res. , vol.22 , pp. 627-633
    • Endo, F.1    Motohara, K.2    Indo, Y.3    Matsuda, I.4
  • 14
    • 0026673888 scopus 로고
    • Purification, characterization, and nucleotide sequence of the thermolabile amylase from the antarctic psychrotroph Alteromonas haloplanktis A23
    • Feller, G., T. Lonhienne, C. Deroanne, C. Libioulle, J. V. Beeumen, and C. Gerday. 1992. Purification, characterization, and nucleotide sequence of the thermolabile amylase from the antarctic psychrotroph Alteromonas haloplanktis A23. J. Biol. Chem. 267:5217-5221.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5217-5221
    • Feller, G.1    Lonhienne, T.2    Deroanne, C.3    Libioulle, C.4    Beeumen, J.V.5    Gerday, C.6
  • 15
    • 0006724944 scopus 로고
    • Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp. (ATCC 27551) contain identical opd genes
    • Harper, L. L., C. S. McDaniel, C. E. Miller, and J. R. 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
  • 16
    • 0021144785 scopus 로고
    • Two enzymes for the detoxification of organophosphorus compounds - Sources, similarities, and significance
    • Hoskin, F. C. G., M. A. Kirkish, and K. E. Steinmann. 1984. Two enzymes for the detoxification of organophosphorus compounds - sources, similarities, and significance. Fund. Appl. Toxicol. 4:165-172.
    • (1984) Fund. Appl. Toxicol. , vol.4 , pp. 165-172
    • Hoskin, F.C.G.1    Kirkish, M.A.2    Steinmann, K.E.3
  • 17
    • 0020037124 scopus 로고
    • Hydrolysis of nerve gas by squid type diisopropylphosphorofluoridate hydrolyzing enzyme on agarose resin
    • Hoskin, F. C. G., and A. H. Roush. 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.G.1    Roush, A.H.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0000911309 scopus 로고
    • Enzymatic hydrolysis of toxic organofluorophosphate compounds
    • Landis, W. G., and J. J. DeFrank. 1990. Enzymatic hydrolysis of toxic organofluorophosphate compounds. Adv. Appl. Biotechnol. Ser. 4:183-201.
    • (1990) Adv. Appl. Biotechnol. Ser. , vol.4 , pp. 183-201
    • Landis, W.G.1    DeFrank, J.J.2
  • 20
    • 15844363269 scopus 로고
    • Purification and characterization of organophosphorus acid anhydrolase from Alteromonas haloplanktis C and Alteromonas sp. M
    • U.S. Army Edgewood Research, Development and Engineering Center, Aberdeen Proving Ground, Md
    • Liu, L., J. Wu, B. Wang, and D. M. Anderson. 1995. Purification and characterization of organophosphorus acid anhydrolase from Alteromonas haloplanktis C and Alteromonas sp. M, p. 12. In International Workshop on Biocatalytic Degradation of Chemical Warfare Related Materials. U.S. Army Edgewood Research, Development and Engineering Center, Aberdeen Proving Ground, Md.
    • (1995) International Workshop on Biocatalytic Degradation of Chemical Warfare Related Materials , pp. 12
    • Liu, L.1    Wu, J.2    Wang, B.3    Anderson, D.M.4
  • 22
    • 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. 164:271-286.
    • (1946) J. Biol. Chem. , vol.164 , pp. 271-286
    • Mazur, A.1
  • 23
    • 0024008341 scopus 로고
    • Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase
    • McDaniel, C. S., L. L. Harper, and J. R. Wild. 1989. Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase. J. Bacteriol. 170:2306-2311.
    • (1989) J. Bacteriol. , vol.170 , pp. 2306-2311
    • McDaniel, C.S.1    Harper, L.L.2    Wild, J.R.3
  • 24
    • 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
  • 25
    • 0022479569 scopus 로고
    • Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by Southern hybridization with opd from Pseudomonas diminuta
    • Mulbry, W., J. S. Karns, P. C. Kearney, J. O. Nelson, C. S. McDaniel, and J. R. Wild. 1986. Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by Southern hybridization with opd from Pseudomonas diminuta. Appl. Environ. Microbiol. 51:926-930.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 926-930
    • Mulbry, W.1    Karns, J.S.2    Kearney, P.C.3    Nelson, J.O.4    McDaniel, C.S.5    Wild, J.R.6
  • 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
  • 28
    • 0023774901 scopus 로고
    • EZ-FIT: A practical curve-fitting microcomputer program for the analysis of enzyme kinetic data on IBM-PC compatible computers
    • 2S. Perella, F. W. 1980. EZ-FIT: a practical curve-fitting microcomputer program for the analysis of enzyme kinetic data on IBM-PC compatible computers. Anal. Biochem. 174:437-447.
    • (1980) Anal. Biochem. , vol.174 , pp. 437-447
    • Perella, F.W.1
  • 29
    • 3543098323 scopus 로고
    • Disorders of proline and hydroxyproline metabolism
    • J. B. Stanbury, J. B. Wyngaarden, D. S. Fredrickson, J. L. Goldstein, and M. S. Brown (ed.), McGraw-Hill Book Co., New York
    • Scriver, R. C., R. J. Smith, and J. M. Phang. 1983. Disorders of proline and hydroxyproline metabolism, p. 360-381. In J. B. Stanbury, J. B. Wyngaarden, D. S. Fredrickson, J. L. Goldstein, and M. S. Brown (ed.), The metabolic basis of inherited disease. McGraw-Hill Book Co., New York.
    • (1983) The Metabolic Basis of Inherited Disease , pp. 360-381
    • Scriver, R.C.1    Smith, R.J.2    Phang, J.M.3
  • 31
    • 0024284551 scopus 로고
    • λZAP: A bacteriophage λ expression vector with in vivo excision properties
    • Short, J. M., J. M. Fernandez, J. A. Sorge, and W. D. Huse. 1988. λZAP: a bacteriophage λ expression vector with in vivo excision properties. Nucleic Acids Res. 16:7583-7589.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7583-7589
    • Short, J.M.1    Fernandez, J.M.2    Sorge, J.A.3    Huse, W.D.4
  • 32
    • 0024523334 scopus 로고
    • Sequencing and high expression of aminopeptidase P gene from Escherichia coli HB101
    • Yoshimoto, T., H. Tone, T. Honda, K. Osatomi, R. Kobayashi, and D. Ysuru. 1989. Sequencing and high expression of aminopeptidase P gene from Escherichia coli HB101. J. Biochem. 105:412-416.
    • (1989) J. Biochem. , vol.105 , pp. 412-416
    • Yoshimoto, T.1    Tone, H.2    Honda, T.3    Osatomi, K.4    Kobayashi, R.5    Ysuru, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.