메뉴 건너뛰기




Volumn 61, Issue , 2007, Pages 233-252

Biocatalysis by Dehalogenating Enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; HALOALKANE DEHALOGENASE; HALOCARBOXYLIC ACID DEHALOGENASE; HALOHYDRIN DEHALOGENASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 34247097923     PISSN: 00652164     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2164(06)61006-X     Document Type: Review
Times cited : (32)

References (62)
  • 1
    • 0032524179 scopus 로고    scopus 로고
    • Synthesis of chiral epihalohydrins using haloalcohol dehalogenase A from Arthrobacter erithii H10a
    • Assis H.M.S., Bull A.T., and Hardman D.J. Synthesis of chiral epihalohydrins using haloalcohol dehalogenase A from Arthrobacter erithii H10a. Enzyme Microb. Technol. 22 (1998) 545-551
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 545-551
    • Assis, H.M.S.1    Bull, A.T.2    Hardman, D.J.3
  • 2
    • 0036300748 scopus 로고    scopus 로고
    • Biodegradation of 1,2,3-trichloropropane through directed evolution and heterologous expression of a haloalkane dehalogenase gene
    • Bosma T., Damborsky J., Stucki G., and Janssen D.B. Biodegradation of 1,2,3-trichloropropane through directed evolution and heterologous expression of a haloalkane dehalogenase gene. Appl. Environ. Microbiol. 68 (2002) 3582-3587
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3582-3587
    • Bosma, T.1    Damborsky, J.2    Stucki, G.3    Janssen, D.B.4
  • 3
    • 0014336317 scopus 로고
    • Biodehalogenation. Epoxidation of halohydrins, epoxide opening, and transhalogenation by a Flavobacterium sp
    • Castro C.E., and Bartnicki E.W. Biodehalogenation. Epoxidation of halohydrins, epoxide opening, and transhalogenation by a Flavobacterium sp. Biochemistry 7 (1968) 3213-3218
    • (1968) Biochemistry , vol.7 , pp. 3213-3218
    • Castro, C.E.1    Bartnicki, E.W.2
  • 4
    • 0346101759 scopus 로고    scopus 로고
    • Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by engineering of its entrance tunnel
    • Chaloupkova R., Sykorova J., Prokop Z., Jesenska A., Monincova M., Pavlova M., Tsuda M., Nagata Y., and Damborsky J. Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by engineering of its entrance tunnel. J. Biol. Chem. 278 (2003) 52622-52628
    • (2003) J. Biol. Chem. , vol.278 , pp. 52622-52628
    • Chaloupkova, R.1    Sykorova, J.2    Prokop, Z.3    Jesenska, A.4    Monincova, M.5    Pavlova, M.6    Tsuda, M.7    Nagata, Y.8    Damborsky, J.9
  • 5
    • 0344295910 scopus 로고
    • The elimination of halide ions from aliphatic halogen-substituted organic acids by an enzyme preparation from Pseudomonas dehalogenans
    • Davies J.I., and Evans W.C. The elimination of halide ions from aliphatic halogen-substituted organic acids by an enzyme preparation from Pseudomonas dehalogenans. Biochem. J. 82 (1962) 50-51
    • (1962) Biochem. J. , vol.82 , pp. 50-51
    • Davies, J.I.1    Evans, W.C.2
  • 8
    • 0346220394 scopus 로고    scopus 로고
    • Structure and mechanism of bacterial dehalogenases: Different ways to cleave a carbon-halogen bond
    • de Jong R.M., and Dijkstra B.W. Structure and mechanism of bacterial dehalogenases: Different ways to cleave a carbon-halogen bond. Curr. Opin Struct. Biol. 13 (2003) 722-730
    • (2003) Curr. Opin Struct. Biol. , vol.13 , pp. 722-730
    • de Jong, R.M.1    Dijkstra, B.W.2
  • 9
    • 0141865521 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial haloalcohol dehalogenase: A new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site
    • de Jong R.M., Tiesinga J.J., Rozeboom H.J., Kalk K.H., Tang L., Janssen D.B., and Dijkstra B.W. Structure and mechanism of a bacterial haloalcohol dehalogenase: A new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site. EMBO J. 22 (2003) 4933-4944
    • (2003) EMBO J. , vol.22 , pp. 4933-4944
    • de Jong, R.M.1    Tiesinga, J.J.2    Rozeboom, H.J.3    Kalk, K.H.4    Tang, L.5    Janssen, D.B.6    Dijkstra, B.W.7
  • 10
    • 25444448270 scopus 로고    scopus 로고
    • Structural basis for the enantioselectivity of an epoxide ring opening reaction catalyzed by haloalcohol dehalogenase HheC
    • de Jong R.M., Tiesinga J.J., Villa A., Tang L., Janssen D.B., and Dijkstra B.W. Structural basis for the enantioselectivity of an epoxide ring opening reaction catalyzed by haloalcohol dehalogenase HheC. J. Am. Chem. Soc. 127 (2005) 13338-13343
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13338-13343
    • de Jong, R.M.1    Tiesinga, J.J.2    Villa, A.3    Tang, L.4    Janssen, D.B.5    Dijkstra, B.W.6
  • 11
    • 33744771679 scopus 로고    scopus 로고
    • The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: Insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family
    • de Jong R.M., Kalk K.H., Tang L., Janssen D.B., and Dijkstra B.W. The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: Insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family. J. Bacteriol. 188 (2006) 4051-4056
    • (2006) J. Bacteriol. , vol.188 , pp. 4051-4056
    • de Jong, R.M.1    Kalk, K.H.2    Tang, L.3    Janssen, D.B.4    Dijkstra, B.W.5
  • 12
    • 0030011754 scopus 로고    scopus 로고
    • Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation
    • Diez A., Prieto M.I., Alvarez M.J., Bautista J.M., Garrido J., and Puyet A. Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation. Biochem. Biophys. Res. Commun. 220 (1996) 828-833
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 828-833
    • Diez, A.1    Prieto, M.I.2    Alvarez, M.J.3    Bautista, J.M.4    Garrido, J.5    Puyet, A.6
  • 13
    • 0035923355 scopus 로고    scopus 로고
    • Haloalkane hydrolysis with an immobilized haloalkane dehalogenase
    • Dravis B.C., Swanson P.E., and Russell A.J. Haloalkane hydrolysis with an immobilized haloalkane dehalogenase. Biotechnol. Bioeng. 75 (2001) 416-423
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 416-423
    • Dravis, B.C.1    Swanson, P.E.2    Russell, A.J.3
  • 14
    • 0028100163 scopus 로고
    • Bacterial dehalogenases: Biochemistry, genetics, and biotechnological applications
    • Fetzner S., and Lingens F. Bacterial dehalogenases: Biochemistry, genetics, and biotechnological applications. Microbiol. Rev. 58 (1994) 641-685
    • (1994) Microbiol. Rev. , vol.58 , pp. 641-685
    • Fetzner, S.1    Lingens, F.2
  • 16
    • 0007579421 scopus 로고
    • The enzymatic cleavage of the carbon-fluorine bond in fluoroacetate
    • Goldman P. The enzymatic cleavage of the carbon-fluorine bond in fluoroacetate. J. Biol. Chem. 240 (1965) 3434-3438
    • (1965) J. Biol. Chem. , vol.240 , pp. 3434-3438
    • Goldman, P.1
  • 19
    • 17844364193 scopus 로고    scopus 로고
    • Nitrite-mediated hydrolysis of epoxides catalyzed by halohydrin dehalogenase from Agrobacterium radiobacter AD1: A new tool for the kinetic resolution of epoxides
    • Hasnaoui G., Lutje Spelberg J.H., De Vries E., Tang L., Hauer B., and Janssen D.B. Nitrite-mediated hydrolysis of epoxides catalyzed by halohydrin dehalogenase from Agrobacterium radiobacter AD1: A new tool for the kinetic resolution of epoxides. Tetr. Asymm. 16 (2005) 1685-1692
    • (2005) Tetr. Asymm. , vol.16 , pp. 1685-1692
    • Hasnaoui, G.1    Lutje Spelberg, J.H.2    De Vries, E.3    Tang, L.4    Hauer, B.5    Janssen, D.B.6
  • 20
    • 0032909021 scopus 로고    scopus 로고
    • Investigation of two evolutionarily unrelated halocarboxylic acid dehalogenase gene families
    • Hill K.E., Marchesi J.R., and Weightman A.J. Investigation of two evolutionarily unrelated halocarboxylic acid dehalogenase gene families. J. Bacteriol. 181 (1999) 2535-2547
    • (1999) J. Bacteriol. , vol.181 , pp. 2535-2547
    • Hill, K.E.1    Marchesi, J.R.2    Weightman, A.J.3
  • 21
    • 0029786674 scopus 로고    scopus 로고
    • Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An α/β hydrolase structure that is different from the α/β hydrolase fold
    • Hisano T., Hata Y., Fujii T., Liu J.Q., Kurihara T., Esaki N., and Soda K. Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An α/β hydrolase structure that is different from the α/β hydrolase fold. J. Biol. Chem. 23 (1996) 20322-20330
    • (1996) J. Biol. Chem. , vol.23 , pp. 20322-20330
    • Hisano, T.1    Hata, Y.2    Fujii, T.3    Liu, J.Q.4    Kurihara, T.5    Esaki, N.6    Soda, K.7
  • 22
    • 1842479420 scopus 로고    scopus 로고
    • Evolving haloalkane dehalogenases
    • Janssen D.B. Evolving haloalkane dehalogenases. Curr. Opin. Chem. Biol. 8 (2004) 150-159
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 150-159
    • Janssen, D.B.1
  • 24
    • 28644444340 scopus 로고    scopus 로고
    • Bacterial degradation of xenobiotic compounds: Evolution and distribution of novel enzyme activities
    • Janssen D.B., Dinkla I.J., Poelarends G.J., and Terpstra P. Bacterial degradation of xenobiotic compounds: Evolution and distribution of novel enzyme activities. Environ. Microbiol. 7 (2005) 1868-1882
    • (2005) Environ. Microbiol. , vol.7 , pp. 1868-1882
    • Janssen, D.B.1    Dinkla, I.J.2    Poelarends, G.J.3    Terpstra, P.4
  • 25
    • 0003134834 scopus 로고
    • Decomposition of chloroacetates and chloropropionates by bacteria
    • Jensen H.L. Decomposition of chloroacetates and chloropropionates by bacteria. Acta Agric. Scand. 10 (1960) 83-103
    • (1960) Acta Agric. Scand. , vol.10 , pp. 83-103
    • Jensen, H.L.1
  • 27
    • 0242438879 scopus 로고    scopus 로고
    • Industrialization of the microbial resolution of chiral C3 and C4 synthetic units: From a small beginning to a major operation, a personal account
    • Kasai N., and Suzuki T. Industrialization of the microbial resolution of chiral C3 and C4 synthetic units: From a small beginning to a major operation, a personal account. Adv. Synth. Catal. 345 (2003) 437-455
    • (2003) Adv. Synth. Catal. , vol.345 , pp. 437-455
    • Kasai, N.1    Suzuki, T.2
  • 28
    • 0031716312 scopus 로고    scopus 로고
    • Optically active chlorohydrins as chiral C3 and C4 building units: Microbial resolution and synthetic applications
    • Kasai N., Suzuki S., and Furukawa Y. Optically active chlorohydrins as chiral C3 and C4 building units: Microbial resolution and synthetic applications. Chirality 10 (1998) 682-692
    • (1998) Chirality , vol.10 , pp. 682-692
    • Kasai, N.1    Suzuki, S.2    Furukawa, Y.3
  • 29
    • 0028116826 scopus 로고
    • Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search
    • Koonin E.V., and Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 18 (1994) 125-132
    • (1994) J. Mol. Biol. , vol.18 , pp. 125-132
    • Koonin, E.V.1    Tatusov, R.L.2
  • 30
    • 0042433495 scopus 로고    scopus 로고
    • Purification, characterization, and gene cloning of a novel fluoroacetate dehalogenase from Burkholderia sp. FA1
    • Kurihara T., Yamauchi T., Ichiyama S., Takahata H., and Esaki N. Purification, characterization, and gene cloning of a novel fluoroacetate dehalogenase from Burkholderia sp. FA1. J. Mol. Catal. B: Enzymatic 23 (2003) 347-355
    • (2003) J. Mol. Catal. B: Enzymatic , vol.23 , pp. 347-355
    • Kurihara, T.1    Yamauchi, T.2    Ichiyama, S.3    Takahata, H.4    Esaki, N.5
  • 31
    • 0032510975 scopus 로고    scopus 로고
    • Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism
    • Li Y.F., Hata Y., Fujii T., Hisano T., Nishihara M., Kurihara T., and Esaki N. Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism. J. Biol. Chem. 12 (1998) 15035-15044
    • (1998) J. Biol. Chem. , vol.12 , pp. 15035-15044
    • Li, Y.F.1    Hata, Y.2    Fujii, T.3    Hisano, T.4    Nishihara, M.5    Kurihara, T.6    Esaki, N.7
  • 35
    • 33645936298 scopus 로고    scopus 로고
    • Enantioselective ring opening of epoxides with cyanide catalysed by halohydrin dehalogenases: A new approach to non racemic β-hydroxynitriles
    • Majerić-Elenkov M., Hauer B., and Janssen D.B. Enantioselective ring opening of epoxides with cyanide catalysed by halohydrin dehalogenases: A new approach to non racemic β-hydroxynitriles. Adv. Synth. Catal. 348 (2006) 579-585
    • (2006) Adv. Synth. Catal. , vol.348 , pp. 579-585
    • Majerić-Elenkov, M.1    Hauer, B.2    Janssen, D.B.3
  • 36
    • 33748992291 scopus 로고    scopus 로고
    • Sequential kinetic resolution catalyzed by halohydrin dehalogenase
    • Majerić Elenkov M., Tang L., Hauer B., and Janssen D.B. Sequential kinetic resolution catalyzed by halohydrin dehalogenase. Org. Lett. 8 (2006) 4227-4229
    • (2006) Org. Lett. , vol.8 , pp. 4227-4229
    • Majerić Elenkov, M.1    Tang, L.2    Hauer, B.3    Janssen, D.B.4
  • 37
    • 12344273661 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of building blocks for statin side chains
    • Müller M. Chemoenzymatic synthesis of building blocks for statin side chains. Angew. Chem. Int. Ed. Engl. 44 (2005) 362-365
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 362-365
    • Müller, M.1
  • 38
    • 0025998074 scopus 로고
    • A new catalytic function of halohydrin hydrogen-halide-lyase, synthesis of beta-hydroxynitriles from epoxides and cyanide
    • Nakamura T., Nagasawa T., Yu F., Watanabe I., and Yamada H. A new catalytic function of halohydrin hydrogen-halide-lyase, synthesis of beta-hydroxynitriles from epoxides and cyanide. Biochem. Biophys. Res. Commun. 15 (1991) 124-130
    • (1991) Biochem. Biophys. Res. Commun. , vol.15 , pp. 124-130
    • Nakamura, T.1    Nagasawa, T.2    Yu, F.3    Watanabe, I.4    Yamada, H.5
  • 39
    • 0026446815 scopus 로고
    • Resolution and some properties of enzymes involved in enantioselective transformation of 1,3-dichloro-2-propanol to (R)-3-chloro-1,2-propanediol by Corynebacterium sp. strain N-1074
    • Nakamura T., Nagasawa T., Yu F., Watanabe I., and Yamada H. Resolution and some properties of enzymes involved in enantioselective transformation of 1,3-dichloro-2-propanol to (R)-3-chloro-1,2-propanediol by Corynebacterium sp. strain N-1074. J. Bacteriol. 174 (1992) 7613-7619
    • (1992) J. Bacteriol. , vol.174 , pp. 7613-7619
    • Nakamura, T.1    Nagasawa, T.2    Yu, F.3    Watanabe, I.4    Yamada, H.5
  • 40
    • 0028049579 scopus 로고
    • A new enzymatic synthesis of (R)-γ-chloro-β-hydroxybutyronitrile
    • Nakamura T., Nagasawa T., Yu F., Watanabe I., and Yamada H. A new enzymatic synthesis of (R)-γ-chloro-β-hydroxybutyronitrile. Tetrahedron 50 (1994) 11821-11826
    • (1994) Tetrahedron , vol.50 , pp. 11821-11826
    • Nakamura, T.1    Nagasawa, T.2    Yu, F.3    Watanabe, I.4    Yamada, H.5
  • 41
    • 0030760868 scopus 로고    scopus 로고
    • Bacterial DL-2-haloacid dehalogenase from Pseudomonas sp. strain 113: Gene cloning and structural comparison with D- and L-2-haloacid dehalogenases
    • Nardi-Dei V., Kurihara T., Park C., Esaki N., and Soda K. Bacterial DL-2-haloacid dehalogenase from Pseudomonas sp. strain 113: Gene cloning and structural comparison with D- and L-2-haloacid dehalogenases. J. Bacteriol. 79 (1997) 4232-4238
    • (1997) J. Bacteriol. , vol.79 , pp. 4232-4238
    • Nardi-Dei, V.1    Kurihara, T.2    Park, C.3    Esaki, N.4    Soda, K.5
  • 42
    • 0033597883 scopus 로고    scopus 로고
    • DL-2-Haloacid dehalogenase from Pseudomonas sp. 113 is a new class of dehalogenase catalyzing hydrolytic dehalogenation not involving enzyme-substrate ester intermediate
    • Nardi-Dei V., Kurihara T., Park C., Miyagi M., Tsunasawa S., Soda K., and Esaki N. DL-2-Haloacid dehalogenase from Pseudomonas sp. 113 is a new class of dehalogenase catalyzing hydrolytic dehalogenation not involving enzyme-substrate ester intermediate. J. Biol. Chem. 274 (1999) 20977-20981
    • (1999) J. Biol. Chem. , vol.274 , pp. 20977-20981
    • Nardi-Dei, V.1    Kurihara, T.2    Park, C.3    Miyagi, M.4    Tsunasawa, S.5    Soda, K.6    Esaki, N.7
  • 43
    • 0034009308 scopus 로고    scopus 로고
    • Covalent and metal-chelate immobilization of a modified 2-haloacid dehalogenase for the enzymatic resolution of optically active chloropropionic acid
    • Ordaz E., Garrido-Pertierra A., Gallego M., and Puyet A. Covalent and metal-chelate immobilization of a modified 2-haloacid dehalogenase for the enzymatic resolution of optically active chloropropionic acid. Biotechnol. Prog. 16 (2000) 287-291
    • (2000) Biotechnol. Prog. , vol.16 , pp. 287-291
    • Ordaz, E.1    Garrido-Pertierra, A.2    Gallego, M.3    Puyet, A.4
  • 44
    • 0343661307 scopus 로고
    • Immobilisation of the D-2-haloacid dehalogenase from Pseudomonas putida strain AJl/23
    • Parker K., and Colby J. Immobilisation of the D-2-haloacid dehalogenase from Pseudomonas putida strain AJl/23. Biodegradation 6 (1995) 191-201
    • (1995) Biodegradation , vol.6 , pp. 191-201
    • Parker, K.1    Colby, J.2
  • 46
    • 0037092188 scopus 로고    scopus 로고
    • Generating segmental mutations in haloalkane dehalogenase: A novel part in the directed evolution toolbox
    • Pikkemaat M.G., and Janssen D.B. Generating segmental mutations in haloalkane dehalogenase: A novel part in the directed evolution toolbox. Nucleic Acids Res. 30 (2002) e35
    • (2002) Nucleic Acids Res. , vol.30
    • Pikkemaat, M.G.1    Janssen, D.B.2
  • 48
    • 0034098678 scopus 로고    scopus 로고
    • Haloalkane-utilizing Rhodococcus strains isolated from geographically distinct locations possess a highly conserved gene cluster encoding haloalkane catabolism
    • Poelarends G.J., Zandstra M., Bosma T., Kulakov A., Larkin M.J., Marchesi J.R., Weightman A.J., and Janssen D.B. Haloalkane-utilizing Rhodococcus strains isolated from geographically distinct locations possess a highly conserved gene cluster encoding haloalkane catabolism. J. Bacteriol. 182 (2000) 2725-2731
    • (2000) J. Bacteriol. , vol.182 , pp. 2725-2731
    • Poelarends, G.J.1    Zandstra, M.2    Bosma, T.3    Kulakov, A.4    Larkin, M.J.5    Marchesi, J.R.6    Weightman, A.J.7    Janssen, D.B.8
  • 49
    • 0028242876 scopus 로고
    • The role of spontaneous cap domain mutations in haloalkane dehalogenase specificity and evolution
    • Pries F., van den Wijngaard A.J., Bos R., Pentenga M., and Janssen D.B. The role of spontaneous cap domain mutations in haloalkane dehalogenase specificity and evolution. J. Biol. Chem. 269 (1994) 17490-17494
    • (1994) J. Biol. Chem. , vol.269 , pp. 17490-17494
    • Pries, F.1    van den Wijngaard, A.J.2    Bos, R.3    Pentenga, M.4    Janssen, D.B.5
  • 50
    • 34247165303 scopus 로고    scopus 로고
    • Process for preparing optically active haloalkane and alcohols by haloalkane dehalogenase-catalyzed hydrolytic dehalogenation
    • Prokop Z., Damborsky J., Nagata Y., and Janssen D.B. Process for preparing optically active haloalkane and alcohols by haloalkane dehalogenase-catalyzed hydrolytic dehalogenation. Patent application WO2006079295 (2006)
    • (2006) Patent application WO2006079295
    • Prokop, Z.1    Damborsky, J.2    Nagata, Y.3    Janssen, D.B.4
  • 51
    • 0031455377 scopus 로고    scopus 로고
    • Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate
    • Ridder I.S., Rozeboom H.J., Kalk K.H., Janssen D.B., and Dijkstra B.W. Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate. J. Biol. Chem. 272 (1997) 33015-33022
    • (1997) J. Biol. Chem. , vol.272 , pp. 33015-33022
    • Ridder, I.S.1    Rozeboom, H.J.2    Kalk, K.H.3    Janssen, D.B.4    Dijkstra, B.W.5
  • 52
    • 0032724654 scopus 로고    scopus 로고
    • Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase
    • Ridder I.S., Rozeboom H.J., Kalk K.H., and Dijkstra B.W. Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase. J. Biol. Chem. 274 (1999) 30672-30678
    • (1999) J. Biol. Chem. , vol.274 , pp. 30672-30678
    • Ridder, I.S.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 53
    • 0025323854 scopus 로고
    • Purification and characterisation of D-2-haloacid dehalogenase from Pseudomonas putida strain AJl/23
    • Smith J., Harrison K., and Colby J. Purification and characterisation of D-2-haloacid dehalogenase from Pseudomonas putida strain AJl/23. J. Gen. Microbiol. 136 (1990) 881-886
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 881-886
    • Smith, J.1    Harrison, K.2    Colby, J.3
  • 54
    • 0033179546 scopus 로고    scopus 로고
    • Dehalogenases applied to industrial-scale biocatalysis
    • Swanson P.E. Dehalogenases applied to industrial-scale biocatalysis. Curr. Opin. Biotechnol. 10 (1999) 365-369
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 365-369
    • Swanson, P.E.1
  • 55
    • 0037074924 scopus 로고    scopus 로고
    • Improved stability of halohydrin dehalogenase from Agrobacterium radiobacter AD1 by replacement of cysteine residues
    • Tang L., van Hylckama Vlieg J.E.T., Fraaije M., and Janssen D.B. Improved stability of halohydrin dehalogenase from Agrobacterium radiobacter AD1 by replacement of cysteine residues. Enz. Microb. Technol. 30 (2002) 251-258
    • (2002) Enz. Microb. Technol. , vol.30 , pp. 251-258
    • Tang, L.1    van Hylckama Vlieg, J.E.T.2    Fraaije, M.3    Janssen, D.B.4
  • 56
    • 0038219597 scopus 로고    scopus 로고
    • Kinetic mechanism and enantioselectivity of halohydrin dehalogenase from Agrobacterium radiobacter
    • Tang L., Lutje Spelberg J.H., Fraaije M.W., and Janssen D.B. Kinetic mechanism and enantioselectivity of halohydrin dehalogenase from Agrobacterium radiobacter. Biochemistry 42 (2003) 5378-5386
    • (2003) Biochemistry , vol.42 , pp. 5378-5386
    • Tang, L.1    Lutje Spelberg, J.H.2    Fraaije, M.W.3    Janssen, D.B.4
  • 57
  • 58
    • 0344222647 scopus 로고    scopus 로고
    • (S)-2-chloropanoic acid: Developments in its industrial manufacture
    • Collins A.N., Sheldrake G.N., and Crosby J. (Eds), John Wiley and Sons, Chichester
    • Taylor S.C. (S)-2-chloropanoic acid: Developments in its industrial manufacture. In: Collins A.N., Sheldrake G.N., and Crosby J. (Eds). "Chirality in Industry II" (1997), John Wiley and Sons, Chichester 207-223
    • (1997) "Chirality in Industry II" , pp. 207-223
    • Taylor, S.C.1
  • 59
    • 33748085677 scopus 로고    scopus 로고
    • Competitors want to get a piece of lipitor
    • Thayer A.M. Competitors want to get a piece of lipitor. Chem. Eng. News 84 (2006) 26-27
    • (2006) Chem. Eng. News , vol.84 , pp. 26-27
    • Thayer, A.M.1
  • 61
    • 0027337615 scopus 로고
    • Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
    • Verschueren K.H., Seljee F., Rozeboom H.J., Kalk K.H., and Dijkstra B.W. Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 363 (1993) 693-698
    • (1993) Nature , vol.363 , pp. 693-698
    • Verschueren, K.H.1    Seljee, F.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 62
    • 0019915696 scopus 로고
    • Stereospecificity of 2-monochloropropionate dehalogenation by the two dehalogenases of Pseudomonas P3: Evidence for two different dehalogenation mechanisms
    • Weightman A.J., Weightman A.L., and Slater J.H. Stereospecificity of 2-monochloropropionate dehalogenation by the two dehalogenases of Pseudomonas P3: Evidence for two different dehalogenation mechanisms. J. Gen. Microbiol. 128 (1982) 1755-1762
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 1755-1762
    • Weightman, A.J.1    Weightman, A.L.2    Slater, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.