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Volumn 237, Issue 2, 1996, Pages 350-356

Muconolactone isomerase of the 3-oxoadipate pathway catalyzes dechlorination of 5-chloro-substituted muconolactones

Author keywords

5 Chloromuconolactone; Alcaligenes eutrophus JMP 134; Dehalogenation; Dienelactone; Muconolactone isomerase

Indexed keywords

ISOMERASE; MUCONOLACTONE DELTA ISOMERASE; ORGANOCHLORINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0029912359     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00350.x     Document Type: Article
Times cited : (25)

References (40)
  • 1
    • 0028784952 scopus 로고
    • From xenobiotic to antibiotic: Formation of protoanenionin by enzymes of the 3-oxoadipate pathway
    • Blasco, R., Wittich, R. M., Mallavarapu, M., Timmis, K. N. & Pieper, D. H. (1995) From xenobiotic to antibiotic: Formation of protoanenionin by enzymes of the 3-oxoadipate pathway, J. Biol. Chem. 270, 29229-29235.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29229-29235
    • Blasco, R.1    Wittich, R.M.2    Mallavarapu, M.3    Timmis, K.N.4    Pieper, D.H.5
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0024971170 scopus 로고
    • Purification and characterization of 4-methylmuconolactone methylisomerase, a novel enzyme of the modified 3-oxoadipate pathway in norcardioform actinomycetes
    • Bruce, N. C., Cain, R. B., Pieper, D. H. & Engesser, K. H. (1989) Purification and characterization of 4-methylmuconolactone methylisomerase, a novel enzyme of the modified 3-oxoadipate pathway in norcardioform actinomycetes, Biochem. J. 262, 303-312.
    • (1989) Biochem. J. , vol.262 , pp. 303-312
    • Bruce, N.C.1    Cain, R.B.2    Pieper, D.H.3    Engesser, K.H.4
  • 4
    • 0014972917 scopus 로고
    • a-butenolide. A 1,2-ring-fission product of 4-methylcatechol by Pseudomonad desmolyticum
    • a-butenolide. A 1,2-ring-fission product of 4-methylcatechol by Pseudomonad desmolyticum, Biochem. J. 121, 89-92.
    • (1971) Biochem. J. , vol.121 , pp. 89-92
    • Catelani, D.1    Fiecchi, A.2    Galli, E.3
  • 6
    • 0014817347 scopus 로고
    • Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins
    • Davies, G. E. & Stark, G. R. (1970) Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins, Proc. Natl Acad. Sci. USA 66, 651-656.
    • (1970) Proc. Natl Acad. Sci. USA , vol.66 , pp. 651-656
    • Davies, G.E.1    Stark, G.R.2
  • 7
    • 0019511050 scopus 로고
    • Properties of six pesticide degradation plasmids isolated from Alcaligenes paradoxus and Alcaligenes eutrophus
    • Don, R. H. & Pemberton, J. M. (1981) Properties of six pesticide degradation plasmids isolated from Alcaligenes paradoxus and Alcaligenes eutrophus, J. Bacteriol. 145, 681-686.
    • (1981) J. Bacteriol. , vol.145 , pp. 681-686
    • Don, R.H.1    Pemberton, J.M.2
  • 8
    • 0017895519 scopus 로고
    • Chemical structure and biodegadability of halogenated aromatic compounds: Two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown Pseudomonad
    • Dorn, E. & Knackmuss, H. J. (1978a) Chemical structure and biodegadability of halogenated aromatic compounds: two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown Pseudomonad, Biochem. J. 174, 73-84.
    • (1978) Biochem. J. , vol.174 , pp. 73-84
    • Dorn, E.1    Knackmuss, H.J.2
  • 9
    • 0017814391 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds: Substituent effects on 1,2-dioxygenation of catechol
    • Dorn, E. & Knackmuss, H.-J. (1978b) Chemical structure and biodegradability of halogenated aromatic compounds: substituent effects on 1,2-dioxygenation of catechol, Biochem. J. 174, 85-94.
    • (1978) Biochem. J. , vol.174 , pp. 85-94
    • Dorn, E.1    Knackmuss, H.-J.2
  • 10
    • 0021636975 scopus 로고
    • Regression analysis of nonlinear Arrhenius plots: An empirical model and a computer program
    • Duggleby, R. G. (1984) Regression analysis of nonlinear Arrhenius plots: an empirical model and a computer program, Comput. Biol. Med. 14, 447-455.
    • (1984) Comput. Biol. Med. , vol.14 , pp. 447-455
    • Duggleby, R.G.1
  • 11
    • 0024280347 scopus 로고
    • Fitting the double Michaelis-Menten equation to kinetic data
    • Duggleby, R. G. (1988) Fitting the double Michaelis-Menten equation to kinetic data, J. Theoret. Biol. 130, 123-124.
    • (1988) J. Theoret. Biol. , vol.130 , pp. 123-124
    • Duggleby, R.G.1
  • 12
    • 0028100163 scopus 로고
    • Bacterial dehalogenases: Biochemistry, genetics, and biotechnical applications
    • Fetzner, S. & Lingens, F. (1994) Bacterial dehalogenases: Biochemistry, genetics, and biotechnical applications, Microb. Rev. 58, 641-685.
    • (1994) Microb. Rev. , vol.58 , pp. 641-685
    • Fetzner, S.1    Lingens, F.2
  • 13
    • 0023655875 scopus 로고
    • Silver staining of native and denatured eucaryotic DNA in agarose gels
    • Gottlieb, M. & Chavko, M. (1987) Silver staining of native and denatured eucaryotic DNA in agarose gels, Anal. Biochem. 165, 33-37.
    • (1987) Anal. Biochem. , vol.165 , pp. 33-37
    • Gottlieb, M.1    Chavko, M.2
  • 14
    • 0018351037 scopus 로고
    • Metabolism of 3-chloro-, 4-chloro-, and 3,5-dichlorobenzoate by a Pseudomonad
    • Hartmann, J., Reineke, W. & Knackmuss, H.-J. (1979) Metabolism of 3-chloro-, 4-chloro-, and 3,5-dichlorobenzoate by a Pseudomonad, Appl. Environ. Microbiol. 37, 421-428.
    • (1979) Appl. Environ. Microbiol. , vol.37 , pp. 421-428
    • Hartmann, J.1    Reineke, W.2    Knackmuss, H.-J.3
  • 15
    • 0022429469 scopus 로고
    • Low resolution crystal structure of muconolactone isomerase. A decamer with a 5-fold symmetry axis
    • Katz, B. A., Ollis, D. & Wyckoff, H. W. (1985) Low resolution crystal structure of muconolactone isomerase. A decamer with a 5-fold symmetry axis, J. Mol. Biol. 184, 311-318.
    • (1985) J. Mol. Biol. , vol.184 , pp. 311-318
    • Katz, B.A.1    Ollis, D.2    Wyckoff, H.W.3
  • 16
    • 0017169760 scopus 로고
    • Cometabolism of 3-methylbenzoate and methylcatechols by a 3-chlorobenzoate utilizing Pseudomonas: Accumulation of (+)-2,5-dihydro2-methyl-5-oxo-furan-2-acetic acid
    • Knackmuss, H.-J., Hellwig, M., Lackner, H. & Otting, W. (1976) Cometabolism of 3-methylbenzoate and methylcatechols by a 3-chlorobenzoate utilizing Pseudomonas: Accumulation of (+)-2,5-dihydro2-methyl-5-oxo-furan-2-acetic acid, Eur. J. Appl. Microbiol. 2, 267-276.
    • (1976) Eur. J. Appl. Microbiol. , vol.2 , pp. 267-276
    • Knackmuss, H.-J.1    Hellwig, M.2    Lackner, H.3    Otting, W.4
  • 17
    • 0025273166 scopus 로고
    • Purification and characterization of dichloromuconate cycloisomerase from Alcaligenes eutrophus JMP 134
    • Kuhm, A. E., Schlömann, M., Knackmuss, H.-J. & Pieper, D. H. (1990) Purification and characterization of dichloromuconate cycloisomerase from Alcaligenes eutrophus JMP 134, Biochem. J. 266, 877.
    • (1990) Biochem. J. , vol.266 , pp. 877
    • Kuhm, A.E.1    Schlömann, M.2    Knackmuss, H.-J.3    Pieper, D.H.4
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 9244235850 scopus 로고
    • DDT dehydrogenase. II. Substrate and cofactor specificity
    • Lipke, H. & Kearns, C. W. (1959) DDT dehydrogenase. II. Substrate and cofactor specificity, J. Biol. Chem. 234, 2129-2132.
    • (1959) J. Biol. Chem. , vol.234 , pp. 2129-2132
    • Lipke, H.1    Kearns, C.W.2
  • 20
    • 0015814279 scopus 로고
    • Relationships among enzymes of the β-ketoadipate pathway: I. Properties of cis, cis-muconate-lactonizing enzyme and muconolactone isomerase from Pseudomonas putida
    • Meagher, R. B. & Ornston, L. N. (1973) Relationships among enzymes of the β-ketoadipate pathway: I. Properties of cis, cis-muconate-lactonizing enzyme and muconolactone isomerase from Pseudomonas putida, Biochemistry 12, 3523-3530.
    • (1973) Biochemistry , vol.12 , pp. 3523-3530
    • Meagher, R.B.1    Ornston, L.N.2
  • 21
    • 0020355754 scopus 로고
    • 3-Chloro-d-analine chloride-lyase (deaminating) of Pseudomonas putida CR 1-1: Purification and charakterization of a novel enzyme occuring in 3-chloro-d-alanine-resistant Pseudomonads
    • Nagasawa, T., Ohkishi, H., Kawakami, B., Yamano, H., Hosano, H., Tani, Y. & Yamada, H. (1982) 3-Chloro-d-analine chloride-lyase (deaminating) of Pseudomonas putida CR 1-1: purification and charakterization of a novel enzyme occuring in 3-chloro-d-alanine-resistant Pseudomonads, J. Biol. Chem. 257, 13749-13756.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13749-13756
    • Nagasawa, T.1    Ohkishi, H.2    Kawakami, B.3    Yamano, H.4    Hosano, H.5    Tani, Y.6    Yamada, H.7
  • 22
    • 0027408819 scopus 로고
    • Stereochemical analysis of γ-HCH degradation by Pseudomonas paucimobilis UT26
    • Nagasawa, S., Kikuchi, R., Nagata, Y., Takagi, M. & Matsuo, M. (1993) Stereochemical analysis of γ-HCH degradation by Pseudomonas paucimobilis UT26, Chemosphere 26, 1187-1201.
    • (1993) Chemosphere , vol.26 , pp. 1187-1201
    • Nagasawa, S.1    Kikuchi, R.2    Nagata, Y.3    Takagi, M.4    Matsuo, M.5
  • 23
    • 0014027888 scopus 로고
    • The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida: I. Biochemistry
    • Ornston, L. N. & Stanier, R. Y. (1966) The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida: I. Biochemistry, J. Biol. Chem. 241, 3776-3786.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3776-3786
    • Ornston, L.N.1    Stanier, R.Y.2
  • 24
    • 0014027930 scopus 로고
    • The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida: III. Enzymes of the catechol pathway
    • Ornston, L. N. (1966) The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida: III. Enzymes of the catechol pathway, J. Biol. Chem. 241, 3795-3799.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3795-3799
    • Ornston, L.N.1
  • 25
    • 85058591889 scopus 로고
    • Recurring themes and repeated sequences in metabolic evolution
    • (Chakrabarty, A. M., ed.) CRC Press, Boca Raton FL
    • Ornston, L. N. & Yeh, W.-K. (1982) Recurring themes and repeated sequences in metabolic evolution, in Biodegradation and detoxification of enviromental pollutants (Chakrabarty, A. M., ed.) pp. 105-126, CRC Press, Boca Raton FL.
    • (1982) Biodegradation and Detoxification of Enviromental Pollutants , pp. 105-126
    • Ornston, L.N.1    Yeh, W.-K.2
  • 26
    • 0018799156 scopus 로고
    • Structual comparison of γ-carboxymuconolactone decarboxylase and muconolactone isomerase from Pseudomonas putida
    • Parke, D. (1979) Structual comparison of γ-carboxymuconolactone decarboxylase and muconolactone isomerase from Pseudomonas putida, Biochim. Biophys. Acta 578, 145-154.
    • (1979) Biochim. Biophys. Acta , vol.578 , pp. 145-154
    • Parke, D.1
  • 27
    • 0016337323 scopus 로고
    • Relationships among enzymes of the β-ketoadipate pathway: IV. Muconolactone isomerase from Acinetobacter calcoaceticus and Pseudomonas putida
    • Patel, R. N., Meagher, R. B. & Ornston, L. N. (1974) Relationships among enzymes of the β-ketoadipate pathway: IV. Muconolactone isomerase from Acinetobacter calcoaceticus and Pseudomonas putida, J. Biol. Chem. 249, 7410-7419.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7410-7419
    • Patel, R.N.1    Meagher, R.B.2    Ornston, L.N.3
  • 28
    • 0022377253 scopus 로고
    • Modified ortho-cleavage pathway in Alcaligenes eutrophus JMP 134 for the degradation of 4-methylcatechol
    • Pieper, D. H., Engesser, K.-H., Don, R. H., Timmis, K. N. & Knackmuss, H.-J. (1985) Modified ortho-cleavage pathway in Alcaligenes eutrophus JMP 134 for the degradation of 4-methylcatechol, FEMS Microbiol. Lett. 29, 63-67.
    • (1985) FEMS Microbiol. Lett. , vol.29 , pp. 63-67
    • Pieper, D.H.1    Engesser, K.-H.2    Don, R.H.3    Timmis, K.N.4    Knackmuss, H.-J.5
  • 29
    • 0024990473 scopus 로고
    • Purification and characterization of 4-methylmuconolactone methylisomerase, a novel enzyme of the modified 3-oxoadipate pathway in the Gram- negative bacterium Alcaligenes eutrophus JMP 134
    • Pieper, D. H., Stadler-Fritzsche, K., Knackmuss, H.-J., Engesser, K.-H., Bruce, N. C. & Cain, R. B. (1990) Purification and characterization of 4-methylmuconolactone methylisomerase, a novel enzyme of the modified 3-oxoadipate pathway in the Gram- negative bacterium Alcaligenes eutrophus JMP 134, Biochem. J. 271, 529-534.
    • (1990) Biochem. J. , vol.271 , pp. 529-534
    • Pieper, D.H.1    Stadler-Fritzsche, K.2    Knackmuss, H.-J.3    Engesser, K.-H.4    Bruce, N.C.5    Cain, R.B.6
  • 30
    • 85050512950 scopus 로고
    • Metabolism of 2-chloro-4-methylphenoxyacetate by Alcaligenes eutrophus JMP 134: Implications for the degradation of chloro- and methyl-substituted aromatics via ortho cleavage
    • (Galli, E., Silver, S. & Witholt, B., eds) American Society for Microbiology, Washington DC
    • Pieper, D. H., Stadler-Fritsche, K., Schlömann, M. & Knackmuss, H.-J. (1992) Metabolism of 2-chloro-4-methylphenoxyacetate by Alcaligenes eutrophus JMP 134: implications for the degradation of chloro- and methyl-substituted aromatics via ortho cleavage, in Pseudomonas: Molecular biology and biotechnology (Galli, E., Silver, S. & Witholt, B., eds) American Society for Microbiology, Washington DC.
    • (1992) Pseudomonas: Molecular Biology and Biotechnology
    • Pieper, D.H.1    Stadler-Fritsche, K.2    Schlömann, M.3    Knackmuss, H.-J.4
  • 31
    • 0027282699 scopus 로고
    • Metabolism of 2-chloro-4-methylphenoxyacetate by Alcaligenes eutrophus JMP 134
    • Pieper, D. H., Stadler-Fritsche, K., Engesser, K. H. & Knackmuss, H. J. (1993) Metabolism of 2-chloro-4-methylphenoxyacetate by Alcaligenes eutrophus JMP 134, Arch. Microbiol. 160, 169-178.
    • (1993) Arch. Microbiol. , vol.160 , pp. 169-178
    • Pieper, D.H.1    Stadler-Fritsche, K.2    Engesser, K.H.3    Knackmuss, H.J.4
  • 32
    • 0029059062 scopus 로고
    • Formation of dimethylmuconolactones from dimethylphenols by Alcaligenes eutrophus JMP 134
    • Pieper, D. H., Stadler-Fritsche, K., Knackmuss, H.-J. & Timmis, K. N. (1995) Formation of dimethylmuconolactones from dimethylphenols by Alcaligenes eutrophus JMP 134, Appl. Environ. Microbiol. 61, 2159-2165.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2159-2165
    • Pieper, D.H.1    Stadler-Fritsche, K.2    Knackmuss, H.-J.3    Timmis, K.N.4
  • 33
    • 0029928157 scopus 로고    scopus 로고
    • Metabolism of 5-chlorosubstituted muconolactones
    • Prucha, M., Vray, V. & Pieper, D. H. (1996) Metabolism of 5-chlorosubstituted muconolactones Eur. J. Biochem 237, 357-366.
    • (1996) Eur. J. Biochem , vol.237 , pp. 357-366
    • Prucha, M.1    Vray, V.2    Pieper, D.H.3
  • 34
    • 0021329184 scopus 로고
    • Microbial metabolism of haloaromatics: Isolation and properties of a chlorobenzene-degrading bacterium
    • Reineke, W. & Knackmuss, H.-J. (1984) Microbial metabolism of haloaromatics: Isolation and properties of a chlorobenzene-degrading bacterium, Appl. Environ. Microbiol. 47, 395-402.
    • (1984) Appl. Environ. Microbiol. , vol.47 , pp. 395-402
    • Reineke, W.1    Knackmuss, H.-J.2
  • 35
  • 36
    • 0025006443 scopus 로고
    • Different types of dienlactone hydrolase in 4-fluorobenzoate-utilizing bacteria
    • Schlömann, M., Schmidt, E. & Knackmuss, H.-J. (1990) Different types of dienlactone hydrolase in 4-fluorobenzoate-utilizing bacteria, J. Bacteriol. 172, 5112-5118.
    • (1990) J. Bacteriol. , vol.172 , pp. 5112-5118
    • Schlömann, M.1    Schmidt, E.2    Knackmuss, H.-J.3
  • 37
    • 0019162442 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid
    • Schmidt, E. & Knackmuss, H.-J. (1980) Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid, Biochem. J. 192, 339-347.
    • (1980) Biochem. J. , vol.192 , pp. 339-347
    • Schmidt, E.1    Knackmuss, H.-J.2
  • 38
    • 0019126978 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds. Halogenated muconic acids as intermediates
    • Schmidt, E., Remberg, G. & Knackmuss, H.-J. (1980) Chemical structure and biodegradability of halogenated aromatic compounds. Halogenated muconic acids as intermediates, Biochem. J. 192, 331-337.
    • (1980) Biochem. J. , vol.192 , pp. 331-337
    • Schmidt, E.1    Remberg, G.2    Knackmuss, H.-J.3
  • 39
    • 0028364164 scopus 로고
    • Inability of muconate cycloisomerase to cause dehalogenation during conversion of 2-chloro-cis,cis-muconate
    • Vollmer, M. D., Fischer, P., Knackmuss, H.-J. & Schlömann, M. (1994) Inability of muconate cycloisomerase to cause dehalogenation during conversion of 2-chloro-cis,cis-muconate, J. Bacteriol. 176, 4366-4375.
    • (1994) J. Bacteriol. , vol.176 , pp. 4366-4375
    • Vollmer, M.D.1    Fischer, P.2    Knackmuss, H.-J.3    Schlömann, M.4
  • 40
    • 0029077739 scopus 로고
    • Conversion of 2-chloro-cis,cis-muconate and its metabolites 2-chloro- and 5-chloromuconolactones by chloromuconate cycloisomerase of pJP4 and pAC27
    • Vollmer, M. D. & Schlömann, M. (1995) Conversion of 2-chloro-cis,cis-muconate and its metabolites 2-chloro- and 5-chloromuconolactones by chloromuconate cycloisomerase of pJP4 and pAC27, J. Bacteriol. 177, 2938-2941.
    • (1995) J. Bacteriol. , vol.177 , pp. 2938-2941
    • Vollmer, M.D.1    Schlömann, M.2


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