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Volumn 103, Issue 6, 2013, Pages 1297-1307

High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production

Author keywords

Catechol 1,2 dioxygenase; cis,cis muconic acid production; Kinetic; Stenotrophomonas; Substrate specificity

Indexed keywords

CATECHOL 1,2 DIOXYGENASE; MUCONIC ACID; PHENOL DERIVATIVE;

EID: 84878300907     PISSN: 00036072     EISSN: 15729699     Source Type: Journal    
DOI: 10.1007/s10482-013-9910-8     Document Type: Article
Times cited : (53)

References (44)
  • 1
    • 0029062188 scopus 로고
    • DO-stat fed-batch production of cis,cis-muconic acid from benzoic acid by Pseudomonas putida BM014
    • 10.1016/0922-338X(95)94001-8 1:CAS:528:DyaK2MXlsVymu7c%3D
    • Bang SG, Choi CY (1995) DO-stat fed-batch production of cis,cis-muconic acid from benzoic acid by Pseudomonas putida BM014. J Ferment Bioeng 79:381-383
    • (1995) J Ferment Bioeng , vol.79 , pp. 381-383
    • Bang, S.G.1    Choi, C.Y.2
  • 2
    • 53349127436 scopus 로고    scopus 로고
    • Production of cis,cis-muconic acid from benzoic acid via microbial transformation
    • 10.1007/BF02949142
    • Bang SG, Choi WJ, Choi CY, Cho MH (1996) Production of cis,cis-muconic acid from benzoic acid via microbial transformation. Biotechnol Bioprocess Eng 1:36-40
    • (1996) Biotechnol Bioprocess Eng , vol.1 , pp. 36-40
    • Bang, S.G.1    Choi, W.J.2    Choi, C.Y.3    Cho, M.H.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method of the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford MM (1976) A rapid and sensitive method of the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-258
    • (1976) Anal Biochem , vol.72 , pp. 248-258
    • Bradford, M.M.1
  • 4
    • 0034468205 scopus 로고    scopus 로고
    • Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens
    • 11307956 10.1023/A:1007116703991 1:CAS:528:DC%2BD3MXit1Ontbs%3D
    • Briganti F, Pessione E, Giunta C, Mazzoli R, Scozzafava A (2000) Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens. J Protein Chem 19:709-716
    • (2000) J Protein Chem , vol.19 , pp. 709-716
    • Briganti, F.1    Pessione, E.2    Giunta, C.3    Mazzoli, R.4    Scozzafava, A.5
  • 5
    • 56549087893 scopus 로고    scopus 로고
    • Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: Recent development in enzymology and modeling studies
    • 19020684 10.1039/b707179p 1:CAS:528:DC%2BD1cXhsVSgsrnM
    • Bruijnincx PCA, van Koten G, Gebbink RJMK (2008) Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: recent development in enzymology and modeling studies. Chem Soc Rev 37:2716-2744
    • (2008) Chem Soc Rev , vol.37 , pp. 2716-2744
    • Bruijnincx, P.C.A.1    Van Koten, G.2    Gebbink, R.3
  • 6
    • 0043022281 scopus 로고    scopus 로고
    • Dioxygenase enzymes: Catalytic mechanisms and chemical models
    • 10.1016/S0040-4020(03)00944-X 1:CAS:528:DC%2BD3sXmsVGhu70%3D
    • Bugg TDH (2003) Dioxygenase enzymes: catalytic mechanisms and chemical models. Tetrahedron 59:7075-7101
    • (2003) Tetrahedron , vol.59 , pp. 7075-7101
    • Bugg, T.D.H.1
  • 7
    • 0035822094 scopus 로고    scopus 로고
    • Solving the riddle of the intradiol and extradiol catechol dioxygenases: How do enzymes control hydroperoxide rearrangements?
    • 10.1039/b100484k
    • Bugg TDH, Lin G (2001) Solving the riddle of the intradiol and extradiol catechol dioxygenases: how do enzymes control hydroperoxide rearrangements? Chem Commun 35:941-952
    • (2001) Chem Commun , vol.35 , pp. 941-952
    • Bugg, T.D.H.1    Lin, G.2
  • 8
    • 0017814391 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds - Substituent effects on 1,2-dioxygenation of catechol
    • 697766 1:CAS:528:DyaE1MXkvFSjtw%3D%3D
    • Dorn E, Knackmuss MJ (1978) 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, M.J.2
  • 10
    • 3042546949 scopus 로고    scopus 로고
    • Crystal structure of 4-chlorocatechol 1,2-dioxygenase from chlorophenol-utilizing Gram-positive Rhodococcus opacus 1CP
    • 15060064 10.1074/jbc.M401692200 1:CAS:528:DC%2BD2cXkvFGnurw%3D
    • Ferraroni M, Solyanikova IP, Kolomytseva MP, Scozzafava A, Golovleva L, Briganti F (2004) Crystal structure of 4-chlorocatechol 1,2-dioxygenase from chlorophenol-utilizing Gram-positive Rhodococcus opacus 1CP. J Biol Chem 279:27646-27655
    • (2004) J Biol Chem , vol.279 , pp. 27646-27655
    • Ferraroni, M.1    Solyanikova, I.P.2    Kolomytseva, M.P.3    Scozzafava, A.4    Golovleva, L.5    Briganti, F.6
  • 13
    • 59349114676 scopus 로고    scopus 로고
    • Catechol 1,2-dioxygenase from α-naphthol degrading thermophilic Geobacillus sp. strain: Purification and properties
    • 10.2478/s11535-008-0049-y 1:CAS:528:DC%2BD1MXht1Oqsbs%3D
    • Giedraityte G, Kalediene L (2009) Catechol 1,2-dioxygenase from α-naphthol degrading thermophilic Geobacillus sp. strain: purification and properties. Cent Eur J Biol 4:68-73
    • (2009) Cent Eur J Biol , vol.4 , pp. 68-73
    • Giedraityte, G.1    Kalediene, L.2
  • 14
    • 67349169177 scopus 로고    scopus 로고
    • Characterization of catechol 1,2-dioxygenase from cell extracts of Sphingomonas xenophaga QYY
    • Guo M, Qu YY, Zhou JT, Li A, Uddin MS (2009) Characterization of catechol 1,2-dioxygenase from cell extracts of Sphingomonas xenophaga QYY. Sci China Ser B-Chem 52:615-620
    • (2009) Sci China ser B-Chem , vol.52 , pp. 615-620
    • Guo, M.1    Qu, Y.Y.2    Zhou, J.T.3    Li, A.4    Uddin, M.S.5
  • 15
    • 79953107665 scopus 로고    scopus 로고
    • Catechol 1,2-dioxygenase from the new aromatic compounds - Degrading Pseudomonas putida strain N6
    • 10.1016/j.ibiod.2011.02.001 1:CAS:528:DC%2BC3MXktFKms74%3D
    • Guzik U, Greń I, Hupert-Kocurek K, Wojcieszyńska D (2011) Catechol 1,2-dioxygenase from the new aromatic compounds - degrading Pseudomonas putida strain N6. Int Biodeter Biodegr 65:504-512
    • (2011) Int Biodeter Biodegr , vol.65 , pp. 504-512
    • Guzik, U.1    Greń, I.2    Hupert-Kocurek, K.3    Wojcieszyńska, D.4
  • 16
    • 79952810842 scopus 로고    scopus 로고
    • High-yield production of cis,cis-muconic acid from catechol in aqueous solution by biocatalyst
    • 10.1246/cl.2011.381 1:CAS:528:DC%2BC3MXptlenu74%3D
    • Kaneko A, Ishii Y, Kirimura K (2011) High-yield production of cis,cis-muconic acid from catechol in aqueous solution by biocatalyst. Chem Lett 40:381-383
    • (2011) Chem Lett , vol.40 , pp. 381-383
    • Kaneko, A.1    Ishii, Y.2    Kirimura, K.3
  • 17
    • 54749141138 scopus 로고    scopus 로고
    • Enhancement of cis,cis-muconate productivity by overexpression of catechol 1,2-dioxygenase in Pseudomonas putida BCM114
    • 10.1007/BF02932513
    • Kim BJ, Choi WJ, Lee EY, Choi CY (1998) Enhancement of cis,cis-muconate productivity by overexpression of catechol 1,2-dioxygenase in Pseudomonas putida BCM114. Biotechnol Bioprocess Eng 3:112-114
    • (1998) Biotechnol Bioprocess Eng , vol.3 , pp. 112-114
    • Kim, B.J.1    Choi, W.J.2    Lee, E.Y.3    Choi, C.Y.4
  • 18
    • 77951498139 scopus 로고    scopus 로고
    • Experimental and theoretical affinity of substituted phenols to chlorocatechol 1,2-dioxygenases: A step toward the comprehension of inhibitor/substrate binding to intradiol dioxygenases
    • 10.1016/j.molcatb.2010.02.001 1:CAS:528:DC%2BC3cXksF2kur4%3D
    • Kolomytseva MP, Ferraroni M, Chernykh AM, Scozzafava A, Briganti F, Golovleva LA (2010) Experimental and theoretical affinity of substituted phenols to chlorocatechol 1,2-dioxygenases: a step toward the comprehension of inhibitor/substrate binding to intradiol dioxygenases. J Mol Catal B-Enzyme 64:53-59
    • (2010) J Mol Catal B-Enzyme , vol.64 , pp. 53-59
    • Kolomytseva, M.P.1    Ferraroni, M.2    Chernykh, A.M.3    Scozzafava, A.4    Briganti, F.5    Golovleva, L.A.6
  • 20
    • 77952582506 scopus 로고    scopus 로고
    • Catechol 1,2-dioxygenase from the gram-positive Rhodococcus opacus 1CP: Quantitative structure/activity relationship and the crystal structures of native enzyme and catechol adducts
    • 10.1016/j.jsb.2009.12.023
    • Matera I, Ferraroni M, Kolomytseva M, Golovleva L, Scozzafava A, Briganti F (2010) Catechol 1,2-dioxygenase from the gram-positive Rhodococcus opacus 1CP: quantitative structure/activity relationship and the crystal structures of native enzyme and catechol adducts. J Struct Biol 170:564-584
    • (2010) J Struct Biol , vol.170 , pp. 564-584
    • Matera, I.1    Ferraroni, M.2    Kolomytseva, M.3    Golovleva, L.4    Scozzafava, A.5    Briganti, F.6
  • 21
    • 4544313536 scopus 로고    scopus 로고
    • Constitutive synthesis, purification, and characterization of catechol 1,2-dioxygenase from the aniline-assimilating bacterium Rhodococcus sp. AN-22
    • 16233669 1:CAS:528:DC%2BD2cXptVKqurs%3D
    • Matsumura E, Ooi S, Murakami S, Takenaka S, Aoki K (2004) Constitutive synthesis, purification, and characterization of catechol 1,2-dioxygenase from the aniline-assimilating bacterium Rhodococcus sp. AN-22. J Biosci Bioeng 98:71-76
    • (2004) J Biosci Bioeng , vol.98 , pp. 71-76
    • Matsumura, E.1    Ooi, S.2    Murakami, S.3    Takenaka, S.4    Aoki, K.5
  • 22
    • 77954142998 scopus 로고    scopus 로고
    • Role of cis,cis-muconic acid in the catalysis of Pseudomonas putida chlorocatechol 1,2-dioxygenase
    • 20452370 10.1016/j.ijbiomac.2010.04.016 1:CAS:528:DC%2BC3cXosV2jtbk%3D
    • Melo FA, Araujo APU, Costa-Filho AJ (2010) Role of cis,cis-muconic acid in the catalysis of Pseudomonas putida chlorocatechol 1,2-dioxygenase. Int J Biol Macromol 47:233-237
    • (2010) Int J Biol Macromol , vol.47 , pp. 233-237
    • Melo, F.A.1    Araujo, A.P.U.2    Costa-Filho, A.J.3
  • 23
    • 0025435189 scopus 로고
    • Microbial production of cis,cis-muconic acid
    • 10.1016/0168-1656(90)90009-Z
    • Mizuno S, Yoshikawa N (1990) Microbial production of cis,cis-muconic acid. J Biotechnol 14:203-210
    • (1990) J Biotechnol , vol.14 , pp. 203-210
    • Mizuno, S.1    Yoshikawa, N.2
  • 24
    • 0032143496 scopus 로고    scopus 로고
    • Purification and characterization of four catechol 1,2-dioxygenase isozymes from the benzamide-assimilating bacterium Arthrobacter species BA-5-17
    • 9760749 10.1016/S0944-5013(98)80036-0 1:CAS:528:DyaK1cXlvV2ls7g%3D
    • Murakami S, Wang CL, Naito A, Shinke R, Aoki K (1998) Purification and characterization of four catechol 1,2-dioxygenase isozymes from the benzamide-assimilating bacterium Arthrobacter species BA-5-17. Microbiol Res 153:163-171
    • (1998) Microbiol Res , vol.153 , pp. 163-171
    • Murakami, S.1    Wang, C.L.2    Naito, A.3    Shinke, R.4    Aoki, K.5
  • 25
    • 84875949401 scopus 로고    scopus 로고
    • Purification and characterization of catechol 1,2-dioxygenase from Rhodocococcus sp. NCIM 2891
    • 1:CAS:528:DC%2BC3MXht1Ciu73I
    • Nadaf NH, Ghosh JS (2011) Purification and characterization of catechol 1,2-dioxygenase from Rhodocococcus sp. NCIM 2891. Res J Environ Earth Sci 3:608-613
    • (2011) Res J Environ Earth Sci , vol.3 , pp. 608-613
    • Nadaf, N.H.1    Ghosh, J.S.2
  • 26
    • 0024094638 scopus 로고    scopus 로고
    • DNA sequence of the Acinetobacter calcoaceticus catechol 1,2-dioxygenase i structural gene catA: Evidence for evolutionary divergence of intradiol dioxygenases by acquisition of DNA sequence repetitions
    • Neidle EL, Hartnett Ch, Bonitz S, Ornston LN (1998) DNA sequence of the Acinetobacter calcoaceticus catechol 1,2-dioxygenase I structural gene catA: evidence for evolutionary divergence of intradiol dioxygenases by acquisition of DNA sequence repetitions. J Bacteriol 170:4874-4880
    • (1998) J Bacteriol , vol.170 , pp. 4874-4880
    • Neidle, E.L.1    Hartnett, C.2    Bonitz, S.3    Ornston, L.N.4
  • 27
    • 0028067892 scopus 로고
    • Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 Å resolution
    • 7990141 10.1006/jmbi.1994.1754 1:CAS:528:DyaK2MXislegtLg%3D
    • Ohlendorf DH, Orville AM, Lipscomb JD (1994) Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 Å resolution. J Mol Biol 244:586-608
    • (1994) J Mol Biol , vol.244 , pp. 586-608
    • Ohlendorf, D.H.1    Orville, A.M.2    Lipscomb, J.D.3
  • 28
    • 0017080224 scopus 로고
    • Catechol 1,2-dioxygenase from Acinetobacter calcoaceticus: Purification and properties
    • 58860 1:CAS:528:DyaE28XltVGrsr8%3D
    • Patel RN, Hou CT, Felix A, Lillard MO (1976) Catechol 1,2-dioxygenase from Acinetobacter calcoaceticus: purification and properties. J Bacteriol 127:536-544
    • (1976) J Bacteriol , vol.127 , pp. 536-544
    • Patel, R.N.1    Hou, C.T.2    Felix, A.3    Lillard, M.O.4
  • 29
    • 41549114161 scopus 로고    scopus 로고
    • Recent applications of biocatalysis in developing green chemistry for chemical synthesis at the industrial scale
    • 10.1039/b716045c 1:CAS:528:DC%2BD1cXjvVegsrs%3D
    • Ran N, Zhao L, Chen Z, Tao J (2008) Recent applications of biocatalysis in developing green chemistry for chemical synthesis at the industrial scale. Green Chem 10:361-372
    • (2008) Green Chem , vol.10 , pp. 361-372
    • Ran, N.1    Zhao, L.2    Chen, Z.3    Tao, J.4
  • 31
    • 0029742386 scopus 로고    scopus 로고
    • Characterisation of chromosomally encoded catechol 1,2-dioxygenase (E.C. 1.13.11.1) from Alcaligenes eutrophus CH34
    • 8661943 10.1007/s002030050353 1:CAS:528:DyaK28XltVWiur8%3D
    • Sauret-Ignazi G, Gagnon J, Béguin J, Barrelle M, Markowicz Y, Pelmont J, Toussaint A (1996) Characterisation of chromosomally encoded catechol 1,2-dioxygenase (E.C. 1.13.11.1) from Alcaligenes eutrophus CH34. Arch Microbiol 166:42-50
    • (1996) Arch Microbiol , vol.166 , pp. 42-50
    • Sauret-Ignazi, G.1    Gagnon, J.2    Béguin, J.3    Barrelle, M.4    Markowicz, Y.5    Pelmont, J.6    Toussaint, A.7
  • 32
    • 13544258806 scopus 로고    scopus 로고
    • Purification and characterization of catechol 1,2-dioxygenase of Pseudomonas fluorescens for degradation of chlorobenzoic acid
    • 1:CAS:528:DC%2BD2MXmtVSiur0%3D
    • Saxena P, Thakur S (2005) Purification and characterization of catechol 1,2-dioxygenase of Pseudomonas fluorescens for degradation of chlorobenzoic acid. Indian J Biotechnol 4:134-138
    • (2005) Indian J Biotechnol , vol.4 , pp. 134-138
    • Saxena, P.1    Thakur, S.2
  • 33
    • 0021719878 scopus 로고
    • Production of cis,cis-muconate from benzoate and fluoro-cis,cis-muconate from 3-fluorobenzoate by benzoate degrading bacteria
    • 10.1007/BF00270599 1:CAS:528:DyaL2MXnslWrtQ%3D%3D
    • Schmidt E, Knackmuss H-J (1984) Production of cis,cis-muconate from benzoate and fluoro-cis,cis-muconate from 3-fluorobenzoate by benzoate degrading bacteria. Appl Microbiol Biotechnol 20:351-355
    • (1984) Appl Microbiol Biotechnol , vol.20 , pp. 351-355
    • Schmidt, E.1    Knackmuss, H.-J.2
  • 34
    • 72449146303 scopus 로고    scopus 로고
    • Methylcatechol 1,2-dioxygenase of Rhodococcus opacus 6a is a new type of the catechol-cleaving enzyme
    • 10.1134/S0006297909090077 1:CAS:528:DC%2BD1MXht1ertLvI
    • Solyanikova IP, Konovalova EI, Golovleva LA (2009) Methylcatechol 1,2-dioxygenase of Rhodococcus opacus 6a is a new type of the catechol-cleaving enzyme. Biochemistry (Moscow) 74:994-1001
    • (2009) Biochemistry (Moscow) , vol.74 , pp. 994-1001
    • Solyanikova, I.P.1    Konovalova, E.I.2    Golovleva, L.A.3
  • 35
    • 0025777419 scopus 로고
    • Pathway for biodegradation of p-nitrophenol in a Moraxella sp
    • 16348446 1:CAS:528:DyaK3MXhvVWrt7c%3D
    • Spain JC, Gibson DT (1991) Pathway for biodegradation of p-nitrophenol in a Moraxella sp. Appl Environ Microbiol 57:812-819
    • (1991) Appl Environ Microbiol , vol.57 , pp. 812-819
    • Spain, J.C.1    Gibson, D.T.2
  • 36
    • 33845641699 scopus 로고    scopus 로고
    • Specificity of catechol ortho-cleavage during para-toluate degradation by Rhodococcus opacus 1CP
    • 10.1134/S0006297906120054 1:CAS:528:DC%2BD28XhtlCjt7nO
    • Suvorova MM, Solyanikova IP, Golovleva LA (2006) Specificity of catechol ortho-cleavage during para-toluate degradation by Rhodococcus opacus 1CP. Biochemistry (Moscow) 71:1316-1323
    • (2006) Biochemistry (Moscow) , vol.71 , pp. 1316-1323
    • Suvorova, M.M.1    Solyanikova, I.P.2    Golovleva, L.A.3
  • 37
    • 0032567402 scopus 로고    scopus 로고
    • Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol
    • 9857017 10.1074/jbc.273.52.34887 1:CAS:528:DyaK1MXisFWqsw%3D%3D
    • Vaillancourt FH, Han S, Fortin PD, Bolin JT, Eltis LD (1998) Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol. J Biol Chem 273:34887-34895
    • (1998) J Biol Chem , vol.273 , pp. 34887-34895
    • Vaillancourt, F.H.1    Han, S.2    Fortin, P.D.3    Bolin, J.T.4    Eltis, L.D.5
  • 38
    • 33746268121 scopus 로고    scopus 로고
    • The ins and outs of ring-cleaving dioxygenases
    • 16849108 10.1080/10409230600817422 1:CAS:528:DC%2BD28XptlCitr4%3D
    • Vaillancourt FH, Bolin JT, Eltis LD (2006) The ins and outs of ring-cleaving dioxygenases. Crit Rev Biochem Mol Biol 41:241-267
    • (2006) Crit Rev Biochem Mol Biol , vol.41 , pp. 241-267
    • Vaillancourt, F.H.1    Bolin, J.T.2    Eltis, L.D.3
  • 39
    • 0014739885 scopus 로고
    • Purification and properties of catechol 1,2-oxygenase from Trichosporon cutaneum
    • 5462291 10.1111/j.1432-1033.1970.tb00869.x 1:CAS:528:DyaE3cXps1yksg%3D%3D
    • Varga JM, Neujahr HY (1970) Purification and properties of catechol 1,2-oxygenase from Trichosporon cutaneum. Eur J Biochem 12:427-434
    • (1970) Eur J Biochem , vol.12 , pp. 427-434
    • Varga, J.M.1    Neujahr, H.Y.2
  • 40
    • 0034654852 scopus 로고    scopus 로고
    • The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker
    • 10801478 10.1016/S0969-2126(00)00122-2 1:CAS:528:DC%2BD3cXivFSis70%3D
    • Vetting MW, Ohlendorf DH (2000) The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker. Structure 8:429-440
    • (2000) Structure , vol.8 , pp. 429-440
    • Vetting, M.W.1    Ohlendorf, D.H.2
  • 41
    • 33646540690 scopus 로고    scopus 로고
    • Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source
    • 10.1016/j.procbio.2006.03.008 1:CAS:528:DC%2BD28XltVKnsr0%3D
    • Wang C-L, You S-L, Wang S-L (2006) Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source. Process Biochem 41:1594-1601
    • (2006) Process Biochem , vol.41 , pp. 1594-1601
    • Wang, C.-L.1    You, S.-L.2    Wang, S.-L.3
  • 42
    • 33947298867 scopus 로고
    • Oxidation of catechol to cis,cis-muconic acid with ozone
    • 10.1021/i360029a011 1:CAS:528:DyaF1MXhtFCmtrY%3D
    • Wingard LB, Finn RK (1969) Oxidation of catechol to cis,cis-muconic acid with ozone. I&EC Product Res Dev 8:65-70
    • (1969) I&EC Product Res Dev , vol.8 , pp. 65-70
    • Wingard, L.B.1    Finn, R.K.2
  • 43
    • 79952572933 scopus 로고    scopus 로고
    • Induction of aromatic ring-cleavage dioxygenases in Stenotrophomonas maltophilia strain KB2 in cometabolic systems
    • 21475727 10.1007/s11274-010-0520-6
    • Wojcieszyńska D, Guzik U, Greń I, Perkosz M, Hupert-Kocurek K (2011) Induction of aromatic ring-cleavage dioxygenases in Stenotrophomonas maltophilia strain KB2 in cometabolic systems. World J Microbiol Biotechnol 27:805-811
    • (2011) World J Microbiol Biotechnol , vol.27 , pp. 805-811
    • Wojcieszyńska, D.1    Guzik, U.2    Greń, I.3    Perkosz, M.4    Hupert-Kocurek, K.5
  • 44
    • 33644980798 scopus 로고    scopus 로고
    • Micriobial synthesis of cis,cis-muconic acid from benzoate by Sphingobacterium sp. mutants
    • 10.1016/j.bej.2005.02.034
    • Wu C-M, Wu C-CSuC-C, Lee S-N, Lee Y-A, Wu J-Y (2006) Micriobial synthesis of cis,cis-muconic acid from benzoate by Sphingobacterium sp. mutants. Biochem Eng J 29:35-40
    • (2006) Biochem Eng J , vol.29 , pp. 35-40
    • Wu, C.-M.1    Wu, C.-C.-C.2    Lee, S.-N.3    Lee, Y.-A.4    Wu, J.-Y.5


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