메뉴 건너뛰기




Volumn 78, Issue 14, 2012, Pages 4995-4998

Biochemical characterization of a novel haloalkane dehalogenase from a cold-adapted bacterium

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL CHARACTERIZATION; COLD-ADAPTED BACTERIA; DEHALOGENASE; ENVIRONMENTAL APPLICATIONS; HIGH ACTIVITY; LOW TEMPERATURES; TEMPERATURE PROFILES;

EID: 84863736380     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00485-12     Document Type: Article
Times cited : (29)

References (35)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, et al. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 3
    • 1842558988 scopus 로고    scopus 로고
    • Relationship of critical temperature to macromolecular synthesis and growth yield in Psychrobacter cryopegella
    • Bakermans C, Nealson KH. 2004. Relationship of critical temperature to macromolecular synthesis and growth yield in Psychrobacter cryopegella. J. Bacteriol. 186:2340-2345.
    • (2004) J. Bacteriol. , vol.186 , pp. 2340-2345
    • Bakermans, C.1    Nealson, K.H.2
  • 4
    • 78049334581 scopus 로고    scopus 로고
    • Development of an enzymatic fiber-optic biosensor for detection of halogenated hydrocarbons
    • Bidmanova S, Chaloupkova R, Damborsky J, Prokop Z. 2010. Development of an enzymatic fiber-optic biosensor for detection of halogenated hydrocarbons. Anal. Bioanal. Chem. 398:1891-1898.
    • (2010) Anal. Bioanal. Chem. , vol.398 , pp. 1891-1898
    • Bidmanova, S.1    Chaloupkova, R.2    Damborsky, J.3    Prokop, Z.4
  • 5
    • 0035313593 scopus 로고    scopus 로고
    • Improved biocatalysts by directed evolution and rational protein design
    • Bornscheuer UT, Pohl M. 2001. Improved biocatalysts by directed evolution and rational protein design. Curr. Opin. Chem. Biol. 5:137-142.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 137-142
    • Bornscheuer, U.T.1    Pohl, M.2
  • 6
    • 33745241399 scopus 로고    scopus 로고
    • Development of a fiber optic enzymatic biosensor for 1 2-dichloroethane
    • Campbell DW, Muller C, Reardon KF. 2006. Development of a fiber optic enzymatic biosensor for 1,2-dichloroethane. Biotechnol. Lett. 28:883-887.
    • (2006) Biotechnol. Lett. , vol.28 , pp. 883-887
    • Campbell, D.W.1    Muller, C.2    Reardon, K.F.3
  • 8
    • 79960577802 scopus 로고    scopus 로고
    • Stereoselectivity and conformational stability of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110: the effect of pH and temperature
    • Chaloupkova R, Prokop Z, Sato Y, Nagata Y, Damborsky J. 2011. Stereoselectivity and conformational stability of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110: the effect of pH and temperature. FEBS J. 278:2728-2738.
    • (2011) FEBS J , vol.278 , pp. 2728-2738
    • Chaloupkova, R.1    Prokop, Z.2    Sato, Y.3    Nagata, Y.4    Damborsky, J.5
  • 10
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: a multiple sequence alignment method with reduced time and space complexity
    • Edgar RC. 2004. MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5:113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 12
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: hot topics in cold adaptation
    • Feller G, Gerday C. 2003. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 1:200-208.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 13
    • 10044222704 scopus 로고    scopus 로고
    • CLANS: a Java application for visualizing protein families based on pairwise similarity
    • Frickey T, Lupas A. 2004. CLANS: a Java application for visualizing protein families based on pairwise similarity. Bioinformatics 20:3702-3704.
    • (2004) Bioinformatics , vol.20 , pp. 3702-3704
    • Frickey, T.1    Lupas, A.2
  • 14
    • 10744230827 scopus 로고    scopus 로고
    • Some like it cold: biocatalysis at low temperatures
    • Georlette D, et al. 2004. Some like it cold: biocatalysis at low temperatures. FEMS Microbiol. Rev. 28:25-42.
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 25-42
    • Georlette, D.1
  • 15
    • 79953208277 scopus 로고    scopus 로고
    • Biochemical characteristics of the novel haloalkane dehalogenase DatA isolated from the plant pathogen Agrobacterium tumefaciens C58
    • Hasan K, et al. 2011. Biochemical characteristics of the novel haloalkane dehalogenase DatA isolated from the plant pathogen Agrobacterium tumefaciens C58. Appl. Environ. Microbiol. 77:1881-1884.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1881-1884
    • Hasan, K.1
  • 16
    • 0001606804 scopus 로고
    • New colorimetric determination of chloride using mercuric thiocyanate and ferric ion
    • Iwasaki I, Utsumi S, Ozawa T. 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
  • 17
    • 1842479420 scopus 로고    scopus 로고
    • Evolving haloalkane dehalogenase
    • Janssen DB. 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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 67651249845 scopus 로고    scopus 로고
    • Biochemical characterization of haloalkane dehalogenase DrbA and DmbC, representatives of a novel subfamily
    • Jesenska A, et al. 2009. Biochemical characterization of haloalkane dehalogenase DrbA and DmbC, representatives of a novel subfamily. Appl. Environ. Microbiol. 75:5157-5160.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 5157-5160
    • Jesenska, A.1
  • 21
    • 0021798672 scopus 로고
    • Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
    • Keuning S, Janssen DB, Witholt B. 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
  • 22
    • 79953165705 scopus 로고    scopus 로고
    • Substrate specificity of haloalkane dehalogenases
    • Koudelakova T, et al. 2011. Substrate specificity of haloalkane dehalogenases. Biochem. J. 435:345-354.
    • (2011) Biochem. J. , vol.435 , pp. 345-354
    • Koudelakova, T.1
  • 23
    • 0031026361 scopus 로고    scopus 로고
    • The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064
    • Kulakova AN, Larkin MJ, Kulakov LA. 1997. The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064. Microbiology 143:109-115.
    • (1997) Microbiology , vol.143 , pp. 109-115
    • Kulakova, A.N.1    Larkin, M.J.2    Kulakov, L.A.3
  • 24
    • 75549086416 scopus 로고    scopus 로고
    • The Genomes On Line Database (GOLD) in 2009 status of genomic and metagenomic projects and their associated metadata
    • Liolios K, et al. 2010. The Genomes On Line Database (GOLD) in 2009: status of genomic and metagenomic projects and their associated metadata. Nucleic Acids Res. 38:D346-D354.
    • (2010) Nucleic Acids Res , vol.38
    • Liolios, K.1
  • 25
    • 34447272975 scopus 로고    scopus 로고
    • The HaloTag: a novel technology for cell imaging and protein analysis
    • Los GV, Wood K. 2007. The HaloTag: a novel technology for cell imaging and protein analysis. Methods Mol. Biol. 356:195-208.
    • (2007) Methods Mol. Biol. , vol.356 , pp. 195-208
    • Los, G.V.1    Wood, K.2
  • 26
    • 0030853537 scopus 로고    scopus 로고
    • Purification and characterization of haloalkane dehalogenase of a new substrate class from a hexachlorohexane-degrading bacterium Sphingomonas paucimobilis UT26
    • Nagata Y, et al. 1997. Purification and characterization of haloalkane dehalogenase of a new substrate class from a hexachlorohexane-degrading bacterium, Sphingomonas paucimobilis UT26. Appl. Environ. Microbiol. 63:3707-3710.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3707-3710
    • Nagata, Y.1
  • 27
    • 68349127373 scopus 로고    scopus 로고
    • HaloTag7: a genetically engineered tag that enhances bacterial expression of soluble proteins and improves protein purification
    • Ohana RF, et al. 2009. HaloTag7: a genetically engineered tag that enhances bacterial expression of soluble proteins and improves protein purification. Protein Expr. Purif. 68:110-120.
    • (2009) Protein Expr. Purif. , vol.68 , pp. 110-120
    • Ohana, R.F.1
  • 28
    • 80054703699 scopus 로고    scopus 로고
    • Comparative void-volume analysis of psychrophilic and mesophilic enzymes: structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility
    • Paredes DI, Watters K, Pitman DJ, Bystroff C, Dordick JS. 2011. Comparative void-volume analysis of psychrophilic and mesophilic enzymes: structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility. BMC Struct. Biol. 11:42.
    • (2011) BMC Struct. Biol. , vol.11 , pp. 42
    • Paredes, D.I.1    Watters, K.2    Pitman, D.J.3    Bystroff, C.4    Dordick, J.S.5
  • 31
    • 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
  • 32
    • 75549088687 scopus 로고    scopus 로고
    • Database resources of the National Center for Biotechnology Information
    • Sayers EW, et al. 2010. Database resources of the National Center for Biotechnology Information. Nucleic Acids Res. 38:D5-D16.
    • (2010) Nucleic Acids Res , vol.38
    • Sayers, E.W.1
  • 33
    • 0029124086 scopus 로고
    • Experiences of a large-scale application of 1 2-dichloroethane degrading microorganisms for groundwater treatment
    • Stucki G, Thuer M. 1995. Experiences of a large-scale application of 1,2-dichloroethane degrading microorganisms for groundwater treatment. Environ. Sci. Technol. 29:2339-2345.
    • (1995) Environ. Sci. Technol. , vol.29 , pp. 2339-2345
    • Stucki, G.1    Thuer, M.2
  • 34
    • 0037590011 scopus 로고    scopus 로고
    • Extremophiles as a source for novel enzymes
    • van den Burg B. 2003. Extremophiles as a source for novel enzymes. Curr. Opin. Microbiol. 6:213-218.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 213-218
    • Van den Burg, B.1
  • 35
    • 82955241462 scopus 로고    scopus 로고
    • Dynamic kinetic resolution process employing haloalkane dehalogenase
    • Westerbeek A, Szymanski W, Feringa BL, Janssen DB. 2011. Dynamic kinetic resolution process employing haloalkane dehalogenase. ACS Catal. 1:1654-1660.
    • (2011) ACS Catal , vol.1 , pp. 1654-1660
    • Westerbeek, A.1    Szymanski, W.2    Feringa, B.L.3    Janssen, D.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.