메뉴 건너뛰기




Volumn 77, Issue 5, 2011, Pages 1881-1884

Biochemical characteristics of the novel haloalkane dehalogenase DatA, isolated from the plant pathogen Agrobacterium tumefaciens C58

Author keywords

[No Author keywords available]

Indexed keywords

AGROBACTERIUM TUMEFACIENS; BIOCHEMICAL CHARACTERISTICS; BIOCHEMICAL CHARACTERIZATION; BROMINATED ALKANES; DEHALOGENASE; DIMERIC STRUCTURE; PLANT PATHOGEN; RACEMIC MIXTURES;

EID: 79953208277     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02109-10     Document Type: Article
Times cited : (31)

References (23)
  • 1
    • 2242469357 scopus 로고    scopus 로고
    • Halide-stabilising residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis
    • Bohac, M., et al. 2002. Halide-stabilising residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis. Biochemistry 41:14272-14280.
    • (2002) Biochemistry , vol.41 , pp. 14272-14280
    • Bohac, M.1
  • 2
    • 20644469267 scopus 로고
    • Quantitative analyses of biochemical kinetic resolutions of enantiomers
    • Chen, C. S., Y. Fujimoto, G. Girdaukas, and C. J. Sih. 1982. Quantitative analyses of biochemical kinetic resolutions of enantiomers. J. Am. Chem. Soc. 104:7294-7299.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7294-7299
    • Chen, C.S.1    Fujimoto, Y.2    Girdaukas, G.3    Sih, C.J.4
  • 4
    • 23944523334 scopus 로고    scopus 로고
    • Microbial enzymes mined from the Urania deep-sea hypersaline anoxic basin
    • Ferrer, M., et al. 2005. Microbial enzymes mined from the Urania deep-sea hypersaline anoxic basin. Chem. Biol. 12:895-904.
    • (2005) Chem. Biol. , vol.12 , pp. 895-904
    • Ferrer, M.1
  • 5
    • 0001606804 scopus 로고
    • New colorimetric determination of chloride using mercuric thiocyanate and ferric ion
    • Iwasaki, I., S. Utsumi, and T. Ozawa. 1952. New colorimetric determination of chloride using mercuric thiocyanate and ferric ion. Bull. Chem. Soc. Jpn. 25:226.
    • (1952) Bull. Chem. Soc. Jpn. , vol.25 , pp. 226
    • Iwasaki, I.1    Utsumi, S.2    Ozawa, T.3
  • 6
    • 1842479420 scopus 로고    scopus 로고
    • Evolving haloalkane dehalogenase
    • Janssen, D. B. 2004. Evolving haloalkane dehalogenase. Curr. Opin. Chem. Biol. 8:150-159.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 150-159
    • Janssen, D.B.1
  • 7
    • 34247097923 scopus 로고    scopus 로고
    • Biocatalysis by dehalogenating enzymes
    • Janssen, D. B. 2007. Biocatalysis by dehalogenating enzymes. Adv. Appl. Microbiol. 61:233-252.
    • (2007) Adv. Appl. Microbiol. , vol.61 , pp. 233-252
    • Janssen, D.B.1
  • 8
    • 0036325189 scopus 로고    scopus 로고
    • Cloning and expression of the haloalkane dehalogenase gene dhmA from Mycobacterium avium N85 and preliminary characterization of DhmA
    • Jesenska, A., et al. 2002. Cloning and expression of the haloalkane dehalogenase gene dhmA from Mycobacterium avium N85 and preliminary characterization of DhmA. Appl. Environ. Microbiol. 68:3724-3730.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3724-3730
    • Jesenska, A.1
  • 9
    • 32044445515 scopus 로고    scopus 로고
    • Cloning, biochemical properties, and distribution of mycobacterial haloalkane dehalogenases
    • Jesenska, A., et al. 2005. Cloning, biochemical properties, and distribution of mycobacterial haloalkane dehalogenases. Appl. Environ. Microbiol. 71:6736-6745.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 6736-6745
    • Jesenska, A.1
  • 10
    • 67651249845 scopus 로고    scopus 로고
    • Biochemical characterization of haloalkane dehalogenase DrbA and DmbC, representative of a novel subfamily
    • Jesenska, A., et al. 2009. Biochemical characterization of haloalkane dehalogenase DrbA and DmbC, representative of a novel subfamily. Appl. Environ. Microbiol. 75:5157-5160.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 5157-5160
    • Jesenska, A.1
  • 11
    • 0021798672 scopus 로고
    • Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
    • Keuning, S., D. B. Janssen, and B. Witholt. 1985. Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. J. Bacteriol. 163:635-639.
    • (1985) J. Bacteriol. , vol.163 , pp. 635-639
    • Keuning, S.1    Janssen, D.B.2    Witholt, B.3
  • 12
    • 0032573194 scopus 로고    scopus 로고
    • Kinetic analysis and X-ray structure of haloalkane dehalogenase with a modified halide-binding site
    • Krooshof, G. H., et al. 1998. Kinetic analysis and X-ray structure of haloalkane dehalogenase with a modified halide-binding site. Biochemistry 37: 15013-15023.
    • (1998) Biochemistry , vol.37 , pp. 15013-15023
    • Krooshof, G.H.1
  • 13
    • 33644877804 scopus 로고    scopus 로고
    • Dissociation/association properties of a dodecameric cyclomaltodextrinase: effect of pH and salt concentration on the oligomeric state
    • Lee, H.-S., et al. 2006. Dissociation/association properties of a dodecameric cyclomaltodextrinase: effect of pH and salt concentration on the oligomeric state. FEBS J. 273:109-121.
    • (2006) FEBS J , vol.273 , pp. 109-121
    • Lee, H.-S.1
  • 14
    • 0030853537 scopus 로고    scopus 로고
    • Purification and characterization of haloalkane dehalogenase of a new substrate class from a γ-hexachlorohexane-degrading bacterium, Sphingomonas paucimobilis UT26
    • Nagata, Y., et al. 1997. Purification and characterization of haloalkane dehalogenase of a new substrate class from a γ-hexachlorohexane-degrading bacterium, Sphingomonas paucimobilis UT26. Appl. Environ. Microbiol. 63: 3707-3710.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3707-3710
    • Nagata, Y.1
  • 15
    • 0033229896 scopus 로고    scopus 로고
    • Construction and characterization of histidine-tagged haloalkane dehalogenase (LinB) of a new substrate class from a γ-hexachlorocyclohexane-degrading bacterium, Sphingomonas paucimobilis UT26
    • Nagata, Y., K. Hynkova, J. Damborsky, and M. Takagi. 1999. Construction and characterization of histidine-tagged haloalkane dehalogenase (LinB) of a new substrate class from a γ-hexachlorocyclohexane-degrading bacterium, Sphingomonas paucimobilis UT26. Protein Expr. Purif. 17:299-304.
    • (1999) Protein Expr. Purif. , vol.17 , pp. 299-304
    • Nagata, Y.1    Hynkova, K.2    Damborsky, J.3    Takagi, M.4
  • 16
    • 32644476853 scopus 로고    scopus 로고
    • Expression of glycosylated haloalkane dehalogenase LinB in Pichia pastoris
    • Nakamura, T., et al. 2006. Expression of glycosylated haloalkane dehalogenase LinB in Pichia pastoris. Protein Expr. Purif. 46:85-91.
    • (2006) Protein Expr. Purif. , vol.46 , pp. 85-91
    • Nakamura, T.1
  • 17
    • 70349330482 scopus 로고    scopus 로고
    • Redesigning dehalogenase access tunnels as a strategy for degrading an anthropogenic substrate
    • Pavlova, M., et al. 2009. Redesigning dehalogenase access tunnels as a strategy for degrading an anthropogenic substrate. Nat. Chem. Biol. 5:727-733.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 727-733
    • Pavlova, M.1
  • 19
    • 70349568479 scopus 로고    scopus 로고
    • pH-temperature-and ion-dependent oligomerization of Sulfolobus solfataricus recombinant amidase: a study with site-specific mutants
    • Politi, L., et al. 2009. pH-, temperature-and ion-dependent oligomerization of Sulfolobus solfataricus recombinant amidase: a study with site-specific mutants. Archaea 2:221-231.
    • (2009) Archaea , vol.2 , pp. 221-231
    • Politi, L.1
  • 20
    • 77956043476 scopus 로고    scopus 로고
    • Enantioselectivity of haloalkane dehalogenases and its modulation by surface loop engineering
    • Prokop, Z., et al. 2010. Enantioselectivity of haloalkane dehalogenases and its modulation by surface loop engineering. Angew. Chem. Int. Ed. 49:6111-6115.
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 6111-6115
    • Prokop, Z.1
  • 21
    • 23744498875 scopus 로고    scopus 로고
    • Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, encode haloalkane dehalogenases with novel structures and substrate specificity
    • Sato, Y., et al. 2005. Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, encode haloalkane dehalogenases with novel structures and substrate specificity. Appl. Environ. Microbiol. 71:4372-4379.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4372-4379
    • Sato, Y.1
  • 22
    • 2342519418 scopus 로고    scopus 로고
    • Hyperthermophilic and salt-dependent formyltransferase from Methanopyrus kandleri
    • Shima, S., R. K. Thauer, and U. Ermler. 2004. Hyperthermophilic and salt-dependent formyltransferase from Methanopyrus kandleri. Biochem. Soc. Trans. 32:269-272.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 269-272
    • Shima, S.1    Thauer, R.K.2    Ermler, U.3
  • 23
    • 0035861496 scopus 로고    scopus 로고
    • The genome of natural genetic engineer Agrobacterium tumefaciens C58
    • Wood, D. W., et al. 2001. The genome of natural genetic engineer Agrobacterium tumefaciens C58. Science 294:2317-2323.
    • (2001) Science , vol.294 , pp. 2317-2323
    • Wood, D.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.