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Volumn 278, Issue 15, 2011, Pages 2728-2738

Stereoselectivity and conformational stability of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110: The effect of pH and temperature

Author keywords

activity; enantioselectivity; haloalkane dehalogenase; oligomerization; pH; structure; thermostability

Indexed keywords

2 BROMOBUTANE; 2 BROMOPENTANE; 2 BROMOPROPIONIC ACID METHYL ESTER; ALICYCLIC COMPOUND; ALKANE DERIVATIVE; ALPHA BROMOESTER DERIVATIVE; BACTERIAL ENZYME; BETA BROMOALKANE DERIVATIVE; BUTYRIC ACID DERIVATIVE; DIMER; ESTER DERIVATIVE; ETHYL 2 BROMOBUTYRATE; HALOALKANE DEHALOGENASE; MONOMER; PROPIONIC ACID DERIVATIVE; PROTEIN DBJA; TETRAMER; UNCLASSIFIED DRUG;

EID: 79960577802     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08203.x     Document Type: Review
Times cited : (23)

References (39)
  • 1
    • 1842479420 scopus 로고    scopus 로고
    • Evolving haloalkane dehalogenases
    • DOI 10.1016/j.cbpa.2004.02.012, PII S1367593104000274
    • Janssen DB, (2004) Evolving haloalkane dehalogenases. Curr Opin Chem Biol 8, 150-159. (Pubitemid 38452429)
    • (2004) Current Opinion in Chemical Biology , vol.8 , Issue.2 , pp. 150-159
    • Janssen, D.B.1
  • 2
    • 0028100163 scopus 로고
    • Bacterial dehalogenases: Biochemistry, genetics, and biotechnological applications
    • Fetzner S, &, Lingens F, (1994) Bacterial dehalogenases: biochemistry, genetics, and biotechnological applications. Microbiol Rev 58, 641-685.
    • (1994) Microbiol Rev , vol.58 , pp. 641-685
    • Fetzner, S.1    Lingens, F.2
  • 3
    • 11044231963 scopus 로고    scopus 로고
    • Biocatalytic synthesis of chiral pharmaceutical intermediates
    • Patel RN, (2004) Biocatalytic synthesis of chiral pharmaceutical intermediates. Food Technol Biotechnol 42, 305-325. (Pubitemid 40044645)
    • (2004) Food Technology and Biotechnology , vol.42 , Issue.4 , pp. 305-325
    • Patel, R.N.1
  • 4
    • 33751078595 scopus 로고    scopus 로고
    • Biocatalysis: Synthesis of chiral intermediates for drugs
    • Patel RN, (2006) Biocatalysis: synthesis of chiral intermediates for drugs. Curr Opin Drug Discov Devel 9, 741-764. (Pubitemid 44761665)
    • (2006) Current Opinion in Drug Discovery and Development , vol.9 , Issue.6 , pp. 741-764
    • Patel, R.N.1
  • 5
    • 23744498875 scopus 로고    scopus 로고
    • Two rizobial srains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, encode haloalkane dehalogenases with novel structures and substrate specificities
    • DOI 10.1128/AEM.71.8.4372-4379.2005
    • Sato Y, Monincova M, Chaloupkova R, Prokop Z, Ohtsubo Y, Minamisawa K, Tsuda M, Damborsky J, &, Nagata Y, (2005) Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, encode haloalkane dehalogenases with novel structures and substrate specificities. Appl Environ Microbiol 71, 4372-4379. (Pubitemid 41129490)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.8 , pp. 4372-4379
    • Sato, Y.1    Monincova, M.2    Chaloupkova, R.3    Prokop, Z.4    Ohtsubo, Y.5    Minamisawa, K.6    Tsuda, M.7    Damborsky, J.8    Nagata, Y.9
  • 8
    • 0037436563 scopus 로고    scopus 로고
    • Dispelling the myths - Biocatalysis in industrial synthesis
    • DOI 10.1126/science.1079237
    • Schoemaker HE, Mink D, &, Wubbolts MG, (2003) Dispelling the myths-biocatalysis in industrial synthesis. Science 299, 1694-1697. (Pubitemid 36337188)
    • (2003) Science , vol.299 , Issue.5613 , pp. 1694-1697
    • Schoemaker, H.E.1    Mink, D.2    WubboLts, M.G.3
  • 9
    • 0035313593 scopus 로고    scopus 로고
    • Improved biocatalysts by directed evolution and rational protein design
    • DOI 10.1016/S1367-5931(00)00182-4
    • Bornscheuer UT, &, Pohl M, (2001) Improved biocatalysts by directed evolution and rational protein design. Curr Opin Chem Biol 5, 137-143. (Pubitemid 32245673)
    • (2001) Current Opinion in Chemical Biology , vol.5 , Issue.2 , pp. 137-143
    • Bornscheuer, U.T.1    Pohl, M.2
  • 10
    • 33846197938 scopus 로고    scopus 로고
    • Biocatalysis for pharmaceutical intermediates: The future is now
    • DOI 10.1016/j.tibtech.2006.12.005, PII S0167779906003131
    • Pollard DJ, &, Woodley JM, (2007) Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol 25, 66-73. (Pubitemid 46109543)
    • (2007) Trends in Biotechnology , vol.25 , Issue.2 , pp. 66-73
    • Pollard, D.J.1    Woodley, J.M.2
  • 11
    • 43649098961 scopus 로고    scopus 로고
    • New opportunities for biocatalysis: Making pharmaceutical processes greener
    • Woodley JM, (2008) New opportunities for biocatalysis: making pharmaceutical processes greener. Trends Biotechnol 26, 321-327.
    • (2008) Trends Biotechnol , vol.26 , pp. 321-327
    • Woodley, J.M.1
  • 12
    • 3543076929 scopus 로고    scopus 로고
    • Enantioselective biocatalysis optimized by directed evolution
    • DOI 10.1016/j.copbio.2004.06.007, PII S0958166904000862
    • Jaeger KE, &, Eggert T, (2004) Enantioselective biocatalysis optimized by directed evolution. Curr Opin Biotechnol 15, 305-313. (Pubitemid 39024691)
    • (2004) Current Opinion in Biotechnology , vol.15 , Issue.4 , pp. 305-313
    • Jaeger, K.-E.1    Eggert, T.2
  • 13
    • 16244379809 scopus 로고    scopus 로고
    • Enhancing catalytic promiscuity for biocatalysis
    • DOI 10.1016/j.cbpa.2005.02.008, Bioorganic Chemistry / Biocatalysis and Biotransformation
    • Kazlauskas RJ, (2005) Enhancing catalytic promiscuity for biocatalysis. Curr Opin Chem Biol 9, 195-201. (Pubitemid 40462490)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.2 , pp. 195-201
    • Kazlauskas, R.J.1
  • 15
    • 0042933795 scopus 로고    scopus 로고
    • Engineered enzymes for improved organic synthesis
    • DOI 10.1016/S0958-1669(03)00095-8
    • Hult K, &, Berglund P, (2003) Engineered enzymes for improved organic synthesis. Curr Opin Biotech 14, 395-400. (Pubitemid 37011319)
    • (2003) Current Opinion in Biotechnology , vol.14 , Issue.4 , pp. 395-400
    • Hult, K.1    Berglund, P.2
  • 16
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen Y-H, Yang JT, &, Martinez HM, (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11, 4120-4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.-H.1    Yang, J.T.2    Martinez, H.M.3
  • 18
    • 1642499126 scopus 로고    scopus 로고
    • Numerical calculation of the pH of maximal protein stability
    • Alexov E, (2004) Numerical calculation of the pH of maximal protein stability. Eur J Biochem 271, 173-185.
    • (2004) Eur J Biochem , vol.271 , pp. 173-185
    • Alexov, E.1
  • 19
    • 4944265460 scopus 로고    scopus 로고
    • Effect of dimer dissociation on activity and thermostability of the α-glucuronidase from Geobacillus stearothermophilus: Dissecting the different oligomeric forms of family 67 glycoside hydrolases
    • DOI 10.1128/JB.186.20.6928-6937.2004
    • Shallom D, Golan G, Shoham G, &, Shoham Y, (2004) Effect of dimer dissociation on activity and thermostability of the α-glucuronidase from Geobacillus stearothermophilus: dissecting the differnt oligomeric forms of family 67 glycoside hydrolases. J Bacteriol 186, 6928-6937. (Pubitemid 39332132)
    • (2004) Journal of Bacteriology , vol.186 , Issue.20 , pp. 6928-6937
    • Shallom, D.1    Golan, G.2    Shoham, G.3    Shoham, Y.4
  • 21
    • 0027337615 scopus 로고
    • Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
    • Verschueren KHG, Seljee F, Rozeboom HJ, Kalk KH, &, Dijkstra BW, (1993) Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 363, 693-698.
    • (1993) Nature , vol.363 , pp. 693-698
    • Verschueren, K.H.G.1    Seljee, F.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 23
    • 0030589167 scopus 로고    scopus 로고
    • Effects of pH on enantiospecificity of alcohol dehydrogenases from Thermoanaerobacter ethanolicus and horse liver
    • DOI 10.1016/S0141-0229(95)00257-X
    • Secundo F, &, Phillips RS, (1996) Effects of pH on enantiospecificity of alcohol dehydrogenases from Thermoanaerobacter ethanolicus and horse liver. Enzyme Microb Technol 19, 487-492. (Pubitemid 26387972)
    • (1996) Enzyme and Microbial Technology , vol.19 , Issue.7 , pp. 487-492
    • Secundo, F.1    Phillips, R.S.2
  • 24
    • 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. (Pubitemid 15008789)
    • (1985) Journal of Bacteriology , vol.163 , Issue.2 , pp. 635-639
    • Keuning, S.1    Janssen, D.B.2    Witholt, B.3
  • 25
    • 0023404069 scopus 로고
    • Purification and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3
    • Yokota T, Omori T, &, Kodama T, (1987) Purification and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3. J Bacteriol 169, 4049-4054.
    • (1987) J Bacteriol , vol.169 , pp. 4049-4054
    • Yokota, T.1    Omori, T.2    Kodama, T.3
  • 26
    • 0036325189 scopus 로고    scopus 로고
    • Cloning and expression of the haloalkane dehalogenase gene dhmA from Mycobacterium avium N85 and preliminary characterization of DhmA
    • DOI 10.1128/AEM.68.8.3724-3730.2002
    • Jesenska A, Bartos M, Czernekova V, Rychlik I, Pavlik I, &, Damborsky J, (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. (Pubitemid 34836678)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.8 , pp. 3724-3730
    • Jesenska, A.1    Bartos, M.2    Czernekova, V.3    Rychlik, I.4    Pavlik, I.5    Damborsky, J.6
  • 29
    • 0030066698 scopus 로고    scopus 로고
    • Temperature modulation of the stereochemistry of enzymatic catalysis: Prospects for exploitation
    • DOI 10.1016/0167-7799(96)80908-5
    • Phillips RS, (1996) Temperature modulation of the stereochemistry of enzymatic catalysis: prospects for exploitation. Trends Biotechnol 14, 13-16. (Pubitemid 26037476)
    • (1996) Trends in Biotechnology , vol.14 , Issue.1 , pp. 13-16
    • Phillips, R.S.1
  • 30
    • 0036102164 scopus 로고    scopus 로고
    • Substrate entropy in enzyme enantioselectivity: An experimental and molecular modeling study of a lipase
    • DOI 10.1110/ps.3480102
    • Ottosson J, Fransson L, &, Hult K, (2002) Substrate entropy in enzyme enantioselectivity: an experimental and molecular modeling study. Protein Sci 11, 1462-1471. (Pubitemid 34547218)
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1462-1471
    • Ottosson, J.1    Fransson, L.2    Hult, K.3
  • 31
    • 0001451237 scopus 로고
    • Temperature-dependent enantiospecificity of secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus
    • Pham VT, Phillips RS, &, Ljungdahl LG, (1989) Temperature-dependent enantiospecificity of secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus. J Am Chem Soc 111, 1935-1936.
    • (1989) J Am Chem Soc , vol.111 , pp. 1935-1936
    • Pham, V.T.1    Phillips, R.S.2    Ljungdahl, L.G.3
  • 32
    • 0032102836 scopus 로고    scopus 로고
    • Enthalpic and entropic contributions to lipase enantioselectivity
    • DOI 10.1016/S0009-3084(98)00031-0, PII S0009308498000310
    • Overbeeke PL, Orrenius C, Jongejan JA, &, Duine JA, (1998) Enthalpic and entropic contributions to lipase enantioselectivity. Chem Phys Lipids 93, 81-93. (Pubitemid 28383207)
    • (1998) Chemistry and Physics of Lipids , vol.93 , Issue.1-2 , pp. 81-93
    • Overbeeke, P.L.A.1    Orrenius, S.C.2    Jongejan, J.A.3    Duine, J.A.4
  • 33
    • 17144452894 scopus 로고    scopus 로고
    • How does active site water affect enzymatic stereorecognition?
    • DOI 10.1016/S1381-1177(02)00156-X, PII S138111770200156X
    • Phillips RS, (2002) How does active site water affect enzymatic stereorecognition? J Mol Catal B Enzym 19-20, 103-107. (Pubitemid 35304724)
    • (2002) Journal of Molecular Catalysis B: Enzymatic , vol.19-20 , pp. 103-107
    • Phillips, R.S.1
  • 34
    • 0031567701 scopus 로고    scopus 로고
    • Temperature effects on S1- and S'1-enantioselectivity of alpha-chymotrypsin
    • Galunsky B, Ignatova S, &, Kasche V, (1997) Temperature effects on S1- and S'1-enantioselectivity of alpha-chymotrypsin. Biochim Biophys Acta 1343, 130-138.
    • (1997) Biochim Biophys Acta , vol.1343 , pp. 130-138
    • Galunsky, B.1    Ignatova, S.2    Kasche, V.3
  • 36
    • 0028302337 scopus 로고
    • Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions
    • Bjellqvist B, Basse B, Olsen E, &, Celis JE, (1994) Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions. Electrophoresis 15, 529-539. (Pubitemid 24151853)
    • (1994) Electrophoresis , vol.15 , Issue.3-4 , pp. 529-539
    • Bjellqvist, B.1    Basse, B.2    Olsen, E.3    Celis, J.E.4
  • 38
    • 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
  • 39
    • 0030853537 scopus 로고    scopus 로고
    • Purification and characterization of a haloalkane dehalogenase of a new substrate class from a γ-hexachlorocyclohexane - Degrading bacterium, Sphingomonas paucimobilis UT26
    • Nagata Y, Miyauchi K, Damborsky J, Manova K, Ansorgova A, &, Takagi M, (1997) Purification and characterization of haloalkane dehalogenase of a new substrate class from a γ-hexachlorocyclohexane-degrading bacterium, Sphingomonas paucimobilis UT26. Appl Environ Microbiol 63, 3707-3710. (Pubitemid 27383176)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.9 , pp. 3707-3710
    • Nagata, Y.1    Miyauchi, K.2    Damborsky, J.3    Manova, K.4    Ansorgova, A.5    Takagi, M.6


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