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Volumn 2, Issue 5, 1998, Pages 613-617

Microbial dehalogenases: Enzymes recruited to convert xenobiotic substrates

Author keywords

[No Author keywords available]

Indexed keywords

2 HALOACID DEHALOGENASE; 2,3,5,6 TETRACHLOROHYDROQUINONE; 2,3,5,6-TETRACHLOROHYDROQUINONE; 2-HALOACID DEHALOGENASE; DICHLOROMETHANE; DICHLOROMETHANE DEHALOGENASE; GLUTATHIONE TRANSFERASE; HALOALKANE DEHALOGENASE; HYDROLASE; HYDROQUINONE DERIVATIVE; LYASE; TETRACHLOROETHYLENE; XENOBIOTIC AGENT;

EID: 0032175395     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(98)80092-6     Document Type: Article
Times cited : (63)

References (39)
  • 2
    • 0025734772 scopus 로고
    • Crystal structure of haloalkane dehalogenase: An enzyme to detoxify halogenated alkanes
    • Franken SM, Rozeboom HJ, Kalk KH, Dijkstra BW: Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes. EMBO J 1991, 10:1297-1302.
    • (1991) EMBO J , vol.10 , pp. 1297-1302
    • Franken, S.M.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 3
    • 0029786674 scopus 로고    scopus 로고
    • Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold
    • Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K: Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold. J Biol Chem 1996, 271:20322-20330.
    • (1996) J Biol Chem , vol.271 , 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
  • 4
    • 0030037645 scopus 로고    scopus 로고
    • Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 a resolution: An enzyme catalyst generated via adaptive mutation
    • Benning MM, Taylor KL, Liu R-Q, Yang G, Xiang H, Wesenberg G, Dunaway-Mariano D, Holden HM: Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 A resolution: an enzyme catalyst generated via adaptive mutation. Biochemistry 1996, 35:8103-8109.
    • (1996) Biochemistry , vol.35 , pp. 8103-8109
    • Benning, M.M.1    Taylor, K.L.2    Liu, R.-Q.3    Yang, G.4    Xiang, H.5    Wesenberg, G.6    Dunaway-Mariano, D.7    Holden, H.M.8
  • 5
    • 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: Purification and characterization of a haloalkane dehalogenase of a new substrate class from a γ-hexachlorocyclohexane-degrading bacterium, Sphingomonas paucimobilis UT26. Appl Environ Microbiol 1997, 63:3707-3710.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3707-3710
    • Nagata, Y.1    Miyauchi, K.2    Damborsky, J.3    Manova, K.4    Ansorgova, A.5    Takagi, M.6
  • 6
    • 0030435054 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of a D,L-haloalkanoic acid dehalogenase encoding gene from Alcaligenes xylosoxidans ssp. denitrificans ABIV
    • Brokamp A, Happe B, Schmidt FRJ: Cloning and nucleotide sequence of a D,L-haloalkanoic acid dehalogenase encoding gene from Alcaligenes xylosoxidans ssp. denitrificans ABIV. Biodegradation 1997, 7:383-396.
    • (1997) Biodegradation , vol.7 , pp. 383-396
    • Brokamp, A.1    Happe, B.2    Schmidt, F.R.J.3
  • 7
    • 0031895255 scopus 로고    scopus 로고
    • Cloning and sequencing of a 2,5-dichlorohydroquinone reductive dehalogenase gene whose product is involved in degradation of gamma-hexachlorocyclohexane by Sphingomonas paucimobilis
    • Miyauchi K, Suh SK, Nagata Y, Takagi M: Cloning and sequencing of a 2,5-dichlorohydroquinone reductive dehalogenase gene whose product is involved in degradation of gamma-hexachlorocyclohexane by Sphingomonas paucimobilis. J Bacteriol 1998, 180:1354-1359. The gene for 2,5-dichlorohydroquinone dehalogenase, linD, has a low level of similarity to the glutathione S-transferase superfamily, and activity in crude extracts is stimulated 3.7-fold by glutathione. This enzyme may be similar to tetrachlorohydroquinone dehalogenase from Sphingomonas chlorophenolica, whose mechanism has been studied in detail.
    • (1998) J Bacteriol , vol.180 , pp. 1354-1359
    • Miyauchi, K.1    Suh, S.K.2    Nagata, Y.3    Takagi, M.4
  • 8
    • 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, 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 1997, 179:4232-4238. This work addresses the function of a 2-haloacid dehalogenase that can dehalogenate both D- and L-2-haloacids, and demonstrates that the enzyme has a single and common active site for dehalogenation of both enantiomers. Catalytically important residues were identified by site-directed mutagenesis of residues conserved between this enzyme and a homologue.
    • (1997) J Bacteriol , vol.179 , pp. 4232-4238
    • Nardi-Dei, V.1    Kurihara, T.2    Park, C.3    Esaki, N.4    Soda, K.5
  • 9
    • 0030756909 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of the broad spectrum chlorobenzene dioxygenase from Burkholderia sp. strain PS12-dechlorination of 1,2,4,5-tetrachlorobenzene
    • Beil S, Happe B, Timmis KN, Pieper DH: Genetic and biochemical characterization of the broad spectrum chlorobenzene dioxygenase from Burkholderia sp. strain PS12-dechlorination of 1,2,4,5-tetrachlorobenzene. Eur J Biochem 1997, 247:190-199.
    • (1997) Eur J Biochem , vol.247 , pp. 190-199
    • Beil, S.1    Happe, B.2    Timmis, K.N.3    Pieper, D.H.4
  • 11
    • 0030806487 scopus 로고    scopus 로고
    • Repositioning the catalytic triad aspartic acid of haloalkane dehalogenase: Effects on stability, kinetics and structure
    • Krooshof GH, Kwant EM, Damborský J, Koca J, Janssen DB: Repositioning the catalytic triad aspartic acid of haloalkane dehalogenase: effects on stability, kinetics and structure. Biochemistry 1997, 36:9571-9580. An insightful examination of the role of the third member of the catalytic triad in haloalkane dehalogenase. Includes a detailed kinetic and structural examination of the multiple effects of changes introduced by site-directed mutagenesis.
    • (1997) Biochemistry , vol.36 , pp. 9571-9580
    • Krooshof, G.H.1    Kwant, E.M.2    Damborský, J.3    Koca, J.4    Janssen, D.B.5
  • 12
  • 14
  • 15
    • 0028942983 scopus 로고
    • Replacement of tryptophan residues in haloalkane dehalogenase reduces halide binding and catalytic activity
    • Kennes C, Pries F, Krooshof GH, Bokma E, Kingma J, Janssen DB: Replacement of tryptophan residues in haloalkane dehalogenase reduces halide binding and catalytic activity. Eur J Biochem 1995, 228:403-407.
    • (1995) Eur J Biochem , vol.228 , pp. 403-407
    • Kennes, C.1    Pries, F.2    Krooshof, G.H.3    Bokma, E.4    Kingma, J.5    Janssen, D.B.6
  • 16
    • 15844362298 scopus 로고    scopus 로고
    • Specificity and kinetics of haloalkane dehalogenase
    • Schanstra J P, Kingma J, Janssen DB: Specificity and kinetics of haloalkane dehalogenase. J Biol Chem 1996, 271:14747-14753.
    • (1996) J Biol Chem , vol.271 , pp. 14747-14753
    • Schanstra, J.P.1    Kingma, J.2    Janssen, D.B.3
  • 17
    • 0029946082 scopus 로고    scopus 로고
    • Kinetics of halide release of haloalkane dehalogenase: Evidence for a slow conformational change
    • Schanstra J, Janssen DB: Kinetics of halide release of haloalkane dehalogenase: Evidence for a slow conformational change. Biochemistry 1996, 35:5624-5632.
    • (1996) Biochemistry , vol.35 , pp. 5624-5632
    • Schanstra, J.1    Janssen, D.B.2
  • 19
    • 0028264374 scopus 로고
    • Reaction of rat liver glutathione-S-transferases and bacterial dichloromethane dehalogenase with dihalomethanes
    • 9. Blocki FA, Logan MSP, Baoli C, Wackett LP: Reaction of rat liver glutathione-S-transferases and bacterial dichloromethane dehalogenase with dihalomethanes. J Biol Chem 1994, 269:8826-8830.
    • (1994) J Biol Chem , vol.269 , pp. 8826-8830
    • Blocki, F.A.1    Logan, M.S.P.2    Baoli, C.3    Wackett, L.P.4
  • 20
    • 0030037613 scopus 로고    scopus 로고
    • Protein engineering studies of dichloromethane dehalogenase/glutathione S-transferase from Methylophilus sp Strain DM11: Serl12 but not Tyr6 is required for enzyme activity
    • Vuilleumier S, Leisinger T: Protein engineering studies of dichloromethane dehalogenase/glutathione S-transferase from Methylophilus sp Strain DM11: Serl12 but not Tyr6 is required for enzyme activity. Eur J Biochem 1996, 239:410-417.
    • (1996) Eur J Biochem , vol.239 , pp. 410-417
    • Vuilleumier, S.1    Leisinger, T.2
  • 21
    • 0031958234 scopus 로고    scopus 로고
    • Effects of bacterial host and dichloromethane dehalogenase on the competitiveness of methylotrophic bacteria growing with dichloromethane
    • Gisi D, Willi L, Traber H, Leisenger T, Vuilleumier S: Effects of bacterial host and dichloromethane dehalogenase on the competitiveness of methylotrophic bacteria growing with dichloromethane. Appl Environ Microbiol 1998, 64:194-1202. The genes for the DM4 and DM11 versions of for dichloromethane dehalogenase were cloned into a dcmA mutant of Methylobacterium sp. strain DM4 in order to allow comparison of the effects of these two genes on bacterial competitiveness in the same genetic background. The competitiveness of Methylobacterium sp. strain DM4 and Methylophilus sp. strain DM11 were also examined.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 194-1202
    • Gisi, D.1    Willi, L.2    Traber, H.3    Leisenger, T.4    Vuilleumier, S.5
  • 22
    • 0025057964 scopus 로고
    • Sequence analysis and expression of the bacterial dichloromethane dehalogenase structural gene, a member of the glutathione S-transferase supergene family
    • La Roche SD, Leisinger T: Sequence analysis and expression of the bacterial dichloromethane dehalogenase structural gene, a member of the glutathione S-transferase supergene family. J Bacteriol 1990, 172:164-171.
    • (1990) J Bacteriol , vol.172 , pp. 164-171
    • La Roche, S.D.1    Leisinger, T.2
  • 23
    • 0028264374 scopus 로고
    • Reaction of rat liver glutathione-S-transferases and bacterial dichloromethane dehalogenase with dihalomethanes
    • Blocki FA, Logan MSP, Baoli C, Wackett LP: Reaction of rat liver glutathione-S-transferases and bacterial dichloromethane dehalogenase with dihalomethanes. J Biol Chem 1994, 269:8826-8830.
    • (1994) J Biol Chem , vol.269 , pp. 8826-8830
    • Blocki, F.A.1    Logan, M.S.P.2    Baoli, C.3    Wackett, L.P.4
  • 24
    • 0024265981 scopus 로고
    • Dichloromethane dehalogenase with improved catalytic activity isolated from a fast-growing dichloromethane-utilizing bacterium
    • Scholtz R, Wackett LP, Egli C, Cook AM, Leisinger T: Dichloromethane dehalogenase with improved catalytic activity isolated from a fast-growing dichloromethane-utilizing bacterium. J Bacteriol 1988, 170:5698-5704.
    • (1988) J Bacteriol , vol.170 , pp. 5698-5704
    • Scholtz, R.1    Wackett, L.P.2    Egli, C.3    Cook, A.M.4    Leisinger, T.5
  • 25
    • 0026743357 scopus 로고
    • Purification and characterization of a tetrachloro-p-hydroquinone reductive dehalogenase from a Flavobacterium sp
    • Xun L, Topp E, Orser CS: Purification and characterization of a tetrachloro-p-hydroquinone reductive dehalogenase from a Flavobacterium sp. J Bacteriol 1992, 174:8003-8007.
    • (1992) J Bacteriol , vol.174 , pp. 8003-8007
    • Xun, L.1    Topp, E.2    Orser, C.S.3
  • 26
    • 0026555180 scopus 로고
    • Glutathione is the reducing agent for the reductive dehalogenation of tetrachloro-p-hydroquinone by extracts from a Flavobacterium sp
    • Xun L, Topp E, Orser CS: Glutathione is the reducing agent for the reductive dehalogenation of tetrachloro-p-hydroquinone by extracts from a Flavobacterium sp. Biochem Biophys Res Commun 1992, 182:361-366.
    • (1992) Biochem Biophys Res Commun , vol.182 , pp. 361-366
    • Xun, L.1    Topp, E.2    Orser, C.S.3
  • 27
    • 0030445133 scopus 로고    scopus 로고
    • Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamily
    • McCarthy DL, Navarrete S, Willett WS, Babbitt PC, Copley SD: Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamily. Biochemistry 1996, 35:14634-14642.
    • (1996) Biochemistry , vol.35 , pp. 14634-14642
    • McCarthy, D.L.1    Navarrete, S.2    Willett, W.S.3    Babbitt, P.C.4    Copley, S.D.5
  • 28
    • 0030670259 scopus 로고    scopus 로고
    • Identification of a covalent intermediate between glutathione and Cysteinel 3 during catalysis by tetrachlorohydroquinone dehalogenase
    • McCarthy DL, Louie DF, Copley SD: Identification of a covalent intermediate between glutathione and Cysteinel 3 during catalysis by tetrachlorohydroquinone dehalogenase. J Am Chem Soc 1997, 119: 11337-11338. This paper shows that the mechanism of tetrachlorohydroquinone dehalogenase involves attack of Cys13 upon a glutathione conjugate to form a mixed disulfide at the active site, which subsequently undergoes a thiol-disulfide exchange reaction with glutathione to form glutathione disulfide and regenerate the free enzyme.
    • (1997) J Am Chem Soc , vol.119 , pp. 11337-11338
    • McCarthy, D.L.1    Louie, D.F.2    Copley, S.D.3
  • 29
    • 0027348081 scopus 로고
    • Thioltransferases
    • Edited by Meister A. New York: John Wiley & Sons;
    • Wells WW, Yang Y, Gan Z-R, Deits TL: Thioltransferases. In Advances in Enzymology, vol 66. Edited by Meister A. New York: John Wiley & Sons; 1993:149-202.
    • (1993) Advances in Enzymology , vol.66 , pp. 149-202
    • Wells, W.W.1    Yang, Y.2    Gan, Z.-R.3    Deits, T.L.4
  • 30
    • 0026799490 scopus 로고
    • Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14S) and its mixed disulfide with glutathione
    • Bushweller JH, Aslund F, Wuthrich K, Holmgren A: Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14S) and its mixed disulfide with glutathione. Biochemistry 1992, 31:9288-9292.
    • (1992) Biochemistry , vol.31 , pp. 9288-9292
    • Bushweller, J.H.1    Aslund, F.2    Wuthrich, K.3    Holmgren, A.4
  • 31
    • 0025788552 scopus 로고
    • Identification and characterization of the functional amino acids at the active site of pig liver thioltransferase by site-directed mutagenesis
    • Yang Y, Wells WW: Identification and characterization of the functional amino acids at the active site of pig liver thioltransferase by site-directed mutagenesis. J Biol Chem 1991, 266:12759-12765.
    • (1991) J Biol Chem , vol.266 , pp. 12759-12765
    • Yang, Y.1    Wells, W.W.2
  • 33
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • Wilce MCJ,Parker MW: Structure and function of glutathione S-transferases. Biochim Biophys Acta 1994, 1205:1-18.
    • (1994) Biochim Biophys Acta , vol.1205 , pp. 1-18
    • Wilce, M.C.J.1    Parker, M.W.2
  • 35
    • 0028831324 scopus 로고
    • Isolation and characterization of Dehalospirillum multivorans gen. nov., sp. nov., a tetrachloroethene-utilizing, strictly anaerobic bacterium
    • Scholz-Muramatsu H, Neumann A, Mebmer M, Moore E, Diekert G: Isolation and characterization of Dehalospirillum multivorans gen. nov., sp. nov., a tetrachloroethene-utilizing, strictly anaerobic bacterium. Arch Microbiol 1995, 163:48-56.
    • (1995) Arch Microbiol , vol.163 , pp. 48-56
    • Scholz-Muramatsu, H.1    Neumann, A.2    Mebmer, M.3    Moore, E.4    Diekert, G.5
  • 36
    • 0029664484 scopus 로고    scopus 로고
    • The proton/electron ration of the menaquinone-dependent electron transport from dihydrogen to tetrachloroethene in 'Dehalobacter restrictu'
    • Schumacher W, Holliger C: The proton/electron ration of the menaquinone-dependent electron transport from dihydrogen to tetrachloroethene in 'Dehalobacter restrictu'. J Bacteriol 1996, 178:2328-2333.
    • (1996) J Bacteriol , vol.178 , pp. 2328-2333
    • Schumacher, W.1    Holliger, C.2
  • 37
    • 0344622120 scopus 로고    scopus 로고
    • Isolation of a bacterium that reductively dechlorinates tetrachloroethene to ethene
    • Maymó-Gatell X, Chien Y, Gossett JM, Zinder, SH.: Isolation of a bacterium that reductively dechlorinates tetrachloroethene to ethene. Science 1997, 276:1568-1571. This paper describes the first pure culture of an anareobic microorganism (Dehalococcoides ethenogenes 195) that is capable of reducing tetrachloroethene, a toxic and potentially carcinogenic groundwater contaminant, to ethene. Previous isolates converted tetrachloroethene only as far as cis-dichloroethene.
    • (1997) Science , vol.276 , pp. 1568-1571
    • Maymó-Gatell, X.1    Chien, Y.2    Gossett, J.M.3    Zinder, S.H.4
  • 38
    • 0031980176 scopus 로고    scopus 로고
    • Reductive dechlorination of tetrachloroethene to ethene by a two-component enzyme pathway
    • Magnuson JK, Stern RV, Gossett JM, Zinder SH, Burris DR: Reductive dechlorination of tetrachloroethene to ethene by a two-component enzyme pathway. Appl Environ Microbiol 1998, 64:1270-1275. The first studies of the characteristics of the perchloroethylene (PCE) and trichloroethylene reductive dehalogenases that are responsible for the reduction of PCE to ethene in Dehalococcoides ethenogenes strain 195.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1270-1275
    • Magnuson, J.K.1    Stern, R.V.2    Gossett, J.M.3    Zinder, S.H.4    Burris, D.R.5
  • 39
    • 0029895362 scopus 로고    scopus 로고
    • Purification and characterization of tetrachloroethene reductive dehalogenase from Dehalospirillum multivorans
    • Neumann A, Wohlfarth G, Diekert G: Purification and characterization of tetrachloroethene reductive dehalogenase from Dehalospirillum multivorans. J Biol Chem 1996, 271:16515-16519.
    • (1996) J Biol Chem , vol.271 , pp. 16515-16519
    • Neumann, A.1    Wohlfarth, G.2    Diekert, G.3


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