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Volumn 90, Issue 1, 2011, Pages 107-116

Metabolic production of a novel polymer feedstock, 3-carboxy muconate, from vanillin

Author keywords

3 Carboxy muconate; Acinetobacter baylyi; Biocatalysis; Metabolic engineering; Unsaturated polyester; Vanillin

Indexed keywords

3-CARBOXY MUCONATE; ACINETOBACTER BAYLYI; BIOCATALYSIS; METABOLIC ENGINEERING; UNSATURATED POLYESTER; VANILLIN;

EID: 79954836117     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-3078-1     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 0034530550 scopus 로고    scopus 로고
    • Identification of Amycolatopsis sp. strain HR167 genes, involved in the bioconversion of ferulic acid to vanillin
    • DOI 10.1007/s002530000431
    • S Achterholt H Priefert A Steinbüchel 2000 Identification of Amycolatopsis sp. strain HR167 genes, involved in the bioconversion of ferulic acid to vanillin Appl Microbiol Biotechnol 54 6 799 807 10.1007/s002530000431 1:CAS:528:DC%2BD3MXkvVWjtA%3D%3D (Pubitemid 32009741)
    • (2000) Applied Microbiology and Biotechnology , vol.54 , Issue.6 , pp. 799-807
    • Achterholt, S.1    Priefert, H.2    Steinbuchel, A.3
  • 2
    • 37049140388 scopus 로고
    • Stereochemistry of β-carboxy- and β-hydroxymethyl-muconic derivatives
    • 10.1039/j39680001483
    • AT Ainsworth GW Kirby 1968 Stereochemistry of β-carboxy- and β-hydroxymethyl-muconic derivatives J Chem Soc C 12 1483 1487 10.1039/j39680001483
    • (1968) J Chem Soc C , vol.12 , pp. 1483-1487
    • Ainsworth, A.T.1    Kirby, G.W.2
  • 4
    • 84864172586 scopus 로고    scopus 로고
    • Borregaard Ingredients. http://www.thetabook.no/b/0-demo/114. It was accessed 4th January 2011
    • Borregaard Ingredients
  • 5
    • 9244231291 scopus 로고    scopus 로고
    • Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase
    • DOI 10.1146/annurev.micro.57.030502.090927
    • CK Brown MW Vetting CA Earhart DH Ohlendorf 2004 Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxyogenase Annu Rev Microbiol 58 555 585 10.1146/annurev.micro.57.030502.090927 1:CAS:528: DC%2BD2cXhtVejsr3N (Pubitemid 39551997)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 555-585
    • Brown, C.K.1    Vetting, M.W.2    Earhart, C.A.3    Ohlendorf, D.H.4
  • 6
    • 0023778061 scopus 로고
    • Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase
    • 1:CAS:528:DyaL1MXhvVKrtbY%3D
    • F Brunel J Davison 1988 Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase J Bacteriol 170 10 4924 4930 1:CAS:528: DyaL1MXhvVKrtbY%3D
    • (1988) J Bacteriol , vol.170 , Issue.10 , pp. 4924-4930
    • Brunel, F.1    Davison, J.2
  • 7
    • 0019769046 scopus 로고
    • Purification and properties of protocatechuate 3,4-dioxygenase from Pseudomonas putida. A new iron to subunit stoichiometry
    • C Bull D Ballou 1981 Purification and properties of protocatechuate 3,4-dioxygenase from Pseudomonas putida. A new iron to subunit stoichiometry J Biol Chem 256 24 12673 12680 1:CAS:528:DyaL3MXmtFKqsL4%3D (Pubitemid 12132906)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.24 , pp. 12673-12680
    • Bull, C.1    Ballou, D.P.2
  • 8
    • 0024226015 scopus 로고
    • Vanillate O-demethylase from Pseudomonas Species
    • W.A. Wood S.T. Kellogg (eds). Academic San Diego. 10.1016/0076-6879(88) 61032-9
    • Buswell JA, Ribbons DW (1988) Vanillate O-demethylase from Pseudomonas Species. In: Wood WA, Kellogg ST (eds) Methods in enzymology: biomass, part B, lignin, pectin and chitin, Academic, San Diego, pp 294-301
    • (1988) Methods in Enzymology: Biomass, Part B, Lignin, Pectin and Chitin , pp. 294-301
    • Buswell, J.A.1    Ribbons, D.W.2
  • 9
    • 0004737292 scopus 로고
    • Bacterial attack on phenolic esters: An enzyme system demethylating vanillic acid
    • 1:CAS:528:DyaF2sXmt1SktQ%3D%3D
    • NJ Cartwright AR Smith 1967 Bacterial attack on phenolic esters: an enzyme system demethylating vanillic acid Biochem J 102 3 826 841 1:CAS:528:DyaF2sXmt1SktQ%3D%3D
    • (1967) Biochem J , vol.102 , Issue.3 , pp. 826-841
    • Cartwright, N.J.1    Smith, A.R.2
  • 10
    • 0001311231 scopus 로고
    • Nitrobenzene and Cupric Oxide Oxidations
    • S.Y. Lin and C.W. Dence, Editors. Springer-Verlag: London
    • Chen CL (1992) Nitrobenzene and Cupric Oxide Oxidations, in Methods in Lignin Chemistry, S.Y. Lin and C.W. Dence, Editors. Springer-Verlag: London p. 316
    • (1992) Methods in Lignin Chemistry , pp. 316
    • Chen, C.L.1
  • 12
    • 0141838179 scopus 로고    scopus 로고
    • Photoinitiated cross-linking of the biodegradable polyester poly(propylene fumarate). Part I. Determination of network structure
    • DOI 10.1021/bm030028d
    • JP Fisher MD Timmer TA Holland D Dean PS Engel AG Mikos 2003 Photoinitiated cross-linking of the biodegradable polyester poly(propylene fumarate). Part I. Determination of network structure Biomacromolecules 4 5 1327 1334 10.1021/bm030028d 1:CAS:528:DC%2BD3sXlt1yhur0%3D (Pubitemid 37184648)
    • (2003) Biomacromolecules , vol.4 , Issue.5 , pp. 1327-1334
    • Fisher, J.P.1    Timmer, M.D.2    Holland, T.A.3    Dean, D.4    Engel, P.S.5    Mikos, A.G.6
  • 13
    • 52949120676 scopus 로고    scopus 로고
    • Purification and characterisation of a 4-hydroxy benzaldehyde dehydrogenase cloned from Acinetobacter baylyi
    • 10.1016/j.enzmictec.2008.07.003 1:CAS:528:DC%2BD1cXht1ShsbjL
    • A Gosling M Zachariou M Straffon 2008 Purification and characterisation of a 4-hydroxy benzaldehyde dehydrogenase cloned from Acinetobacter baylyi Enzyme Microb Technol 43 6 417 422 10.1016/j.enzmictec.2008.07.003 1:CAS:528:DC%2BD1cXht1ShsbjL
    • (2008) Enzyme Microb Technol , vol.43 , Issue.6 , pp. 417-422
    • Gosling, A.1    Zachariou, M.2    Straffon, M.3
  • 15
    • 0029795374 scopus 로고    scopus 로고
    • Theβ -Ketoadipate Pathway and the Biology of Self-Identity
    • Harwood CS, Parales RE (1996) Theβ -Ketoadipate Pathway and the Biology of Self-Identity. Annual Review of Microbiology 50(1): p. 553-590
    • (1996) Annual Review of Microbiology , vol.50 , Issue.1 , pp. 553-590
    • Harwood, C.S.1    Parales, R.E.2
  • 16
    • 0017273546 scopus 로고
    • Protocatechuate 3,4-dioxygenase from Acinetobacter calcoaceticus
    • 10.1021/bi00648a020 1:CAS:528:DyaE28XhtVWgs7c%3D
    • CT Hou MO Lillard RD Schwartz 1976 Protocatechuate 3,4-dioxygenase from Acinetobacter calcoaceticus Biochemistry 15 3 582 588 10.1021/bi00648a020 1:CAS:528:DyaE28XhtVWgs7c%3D
    • (1976) Biochemistry , vol.15 , Issue.3 , pp. 582-588
    • Hou, C.T.1    Lillard, M.O.2    Schwartz, R.D.3
  • 17
    • 2242439334 scopus 로고
    • Studies in the polyoxyphenol series: VII. The oxidation of vanillin with sodium chlorite and chlorine dioxide
    • 10.1139/v55-010 1:CAS:528:DyaG28XksFei
    • RM Husband CD Logan CB Purves 1955 Studies in the polyoxyphenol series: VII. The oxidation of vanillin with sodium chlorite and chlorine dioxide Can J Chem 33 68 81 10.1139/v55-010 1:CAS:528:DyaG28XksFei
    • (1955) Can J Chem , vol.33 , pp. 68-81
    • Husband, R.M.1    Logan, C.D.2    Purves, C.B.3
  • 18
    • 0014503154 scopus 로고
    • Transformation of Acinetobacter calcoaceticus (Bacterium anitratum)
    • 1:CAS:528:DyaF1MXhtVeqsLw%3D
    • E Juni A Janik 1969 Transformation of Acinetobacter calcoaceticus (Bacterium anitratum) J Bacteriol 98 1 281 288 1:CAS:528:DyaF1MXhtVeqsLw%3D
    • (1969) J Bacteriol , vol.98 , Issue.1 , pp. 281-288
    • Juni, E.1    Janik, A.2
  • 19
    • 2142817150 scopus 로고    scopus 로고
    • Principles of biorefineries
    • DOI 10.1007/s00253-003-1537-7
    • Kamm B, Kamm M (2004) Principles of biorefineries. Appl Microbiol Biotechnol 64(2):137-45 (Pubitemid 38553681)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.2 , pp. 137-145
    • Kamm, B.1    Kamm, M.2
  • 20
    • 0346183200 scopus 로고
    • The enzymatic formation of β-carboxymuconic acid
    • 1:CAS:528:DyaG2MXhsF2l
    • DL MacDonald RY Stanier JL Ingraham 1954 The enzymatic formation of β-carboxymuconic acid J Biol Chem 210 809 820 1:CAS:528:DyaG2MXhsF2l
    • (1954) J Biol Chem , vol.210 , pp. 809-820
    • MacDonald, D.L.1    Stanier, R.Y.2    Ingraham, J.L.3
  • 21
    • 0029199530 scopus 로고
    • Escherichia coli electrotransformation
    • J.A. Nickoloff (eds). Humana Totowa
    • Miller EM, Nickoloff JA (1995) Escherichia coli electrotransformation. In: Nickoloff JA (ed) Methods in molecular biology. Humana, Totowa, p 105
    • (1995) Methods in Molecular Biology , pp. 105
    • Miller, E.M.1    Nickoloff, J.A.2
  • 22
    • 0033981219 scopus 로고    scopus 로고
    • Substrate range and genetic analysis of Acinetobacter vanillate demethylase
    • DOI 10.1128/JB.182.5.1383-1389.2000
    • B Morawski A Segura LN Ornston 2000 Substrate range and genetic analysis of Acinetobacter vanillate demethylase J Bacteriol 182 5 1383 1389 10.1128/JB.182.5.1383-1389.2000 1:CAS:528:DC%2BD3cXhtF2lurk%3D (Pubitemid 30104418)
    • (2000) Journal of Bacteriology , vol.182 , Issue.5 , pp. 1383-1389
    • Morawski, B.1    Segura, A.2    Ornston, L.N.3
  • 24
    • 0020607202 scopus 로고
    • Polymers from 1,2-disubstituted ethylenic monomers. V. Radical polymerization of dimethyl maleate in the presence or absence of isomerization catalyst
    • T Otsu O Ito N Toyoda 1983 Polymers from 1,2-disubstituted ethylenic monomers. V. Radical polymerization of dimethyl maleate in the presence or absence of isomerization catalyst J Macromol Sci Chem A19 1 27 39 10.1080/00222338308069420 1:CAS:528:DyaL28XhtlSgt7g%3D (Pubitemid 13527066)
    • (1983) Journal of macromolecular science. Chemistry , vol.A19 , Issue.1 , pp. 27-39
    • Otsu Takayuki1    Ito Osamu2    Toyoda Naoyuki3
  • 25
    • 0141482111 scopus 로고    scopus 로고
    • Hydroxycinnamate (hca) catabolic genes from Acinetobacter sp. strain ADP1 are repressed by HcaR and are induced by hydroxycinnamoyl-coenzyme A thioesters
    • DOI 10.1128/AEM.69.9.5398-5409.2003
    • D Parke LN Ornston 2003 Hydroxycinnamate (hca) catabolic genes from Acinetobacter sp. strain ADP1 are repressed by HcaR and are induced by hydroxycinnamoyl-coenzyme A thioesters Appl Environ Microbiol 69 9 5398 5409 10.1128/AEM.69.9.5398-5409.2003 1:CAS:528:DC%2BD3sXntlSju7o%3D (Pubitemid 37150764)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.9 , pp. 5398-5409
    • Parke, D.1    Ornston, N.2
  • 26
    • 0032925513 scopus 로고    scopus 로고
    • NAD-dependent DNA-binding activity of the bifunctional NadR regulator of Salmonella typhimurium
    • T Penfound JW Foster 1999 NAD-dependent DNA-binding activity of the bifunctional NadR regulator of Salmonella typhimurium J Bacteriol 181 2 648 655 1:CAS:528:DyaK1MXmtlWhtQ%3D%3D (Pubitemid 29045159)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 648-655
    • Penfound, T.1    Foster, J.W.2
  • 27
    • 0030981938 scopus 로고    scopus 로고
    • Molecular characterization of genes of Pseudomonas sp. Strain HR199 involved in bioconversion of vanillin to protocatechuate
    • H Priefert J Rabenhorst A Steinbüchel 1997 Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate J Bacteriol 179 8 2595 2607 1:CAS:528:DyaK2sXis1Wisbk%3D (Pubitemid 27164559)
    • (1997) Journal of Bacteriology , vol.179 , Issue.8 , pp. 2595-2607
    • Priefert, H.1    Rabenhorst, J.2    Steinbuchel, A.3
  • 28
    • 0017672048 scopus 로고
    • Protocatechuate 3,4 dioxygenase. Inhibitor studies and mechanistic implications
    • L Que JD Lipscomb E Munck JM Wood 1977 Protocatechuate 3,4-dioxygenase. Inhibitor studies and mechanistic implications Biochim Biophys Acta 485 1 60 74 1:CAS:528:DyaE1cXhvVWkuw%3D%3D (Pubitemid 8219530)
    • (1977) Biochimica et Biophysica Acta , vol.485 , Issue.1 , pp. 60-74
    • Que Jr., L.1    Lipscomb, J.D.2    Munck, E.3    Wood, J.M.4
  • 31
    • 19744373827 scopus 로고    scopus 로고
    • Effect of different levels of NADH availability on metabolic fluxes of Escherichia coli chemostat cultures in defined medium
    • DOI 10.1016/j.jbiotec.2005.02.006, PII S0168165605000921
    • AM Sánchez GN Bennett K-Y San 2005 Effect of different levels of NADH availability on metabolic fluxes of Escherichia coli chemostat cultures in defined medium J Bacteriol 117 4 395 405 (Pubitemid 40745158)
    • (2005) Journal of Biotechnology , vol.117 , Issue.4 , pp. 395-405
    • Sanchez, A.M.1    Bennett, G.N.2    San, K.-Y.3
  • 32
    • 78651051471 scopus 로고
    • Protocatechuic acid oxidase
    • 1:CAS:528:DyaG2MXhsF2m
    • RY Stanier JL Ingraham 1954 Protocatechuic acid oxidase J Biol Chem 210 2 799 808 1:CAS:528:DyaG2MXhsF2m
    • (1954) J Biol Chem , vol.210 , Issue.2 , pp. 799-808
    • Stanier, R.Y.1    Ingraham, J.L.2
  • 33
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • 10.1016/0022-2836(86)90385-2 1:CAS:528:DyaL28XktlKrsr4%3D
    • F Studier B Moffatt 1986 Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes J Mol Biol 189 1 113 130 10.1016/0022-2836(86)90385-2 1:CAS:528:DyaL28XktlKrsr4%3D
    • (1986) J Mol Biol , vol.189 , Issue.1 , pp. 113-130
    • Studier, F.1    Moffatt, B.2
  • 34
    • 31344474305 scopus 로고    scopus 로고
    • Strategies for protein coexpression in Escherichia coli
    • DOI 10.1038/nmeth0106-55, PII N010655
    • NH Tolia L Joshua-Tor 2006 Strategies for protein coexpression in Escherichia coli Nat Meth 3 55 64 10.1038/nmeth0106-55 1:CAS:528: DC%2BD2MXhtlagur3P (Pubitemid 43135350)
    • (2006) Nature Methods , vol.3 , Issue.1 , pp. 55-64
    • Tolia, N.H.1    Joshua-Tor, L.2
  • 35
    • 0034636805 scopus 로고    scopus 로고
    • Structure of Acinetobacter strain ADP1 protocatechuate 3,4- dioxygenase at 2.2 A resolution: Implications for the mechanism of an intradiol dioxygenase
    • DOI 10.1021/bi000151e
    • MW Vetting DA D'Argenio LN Ornston DH Ohlendorf 2000 Structure of Acinetobacter strain ADP1 protocatechuate 3,4-dioxygenase at 2.2 Å resolution: implications for the mechanism of an intradiol dioxygenase Biochemistry 39 27 7943 7955 10.1021/bi000151e 1:CAS:528:DC%2BD3cXktVahsLY%3D (Pubitemid 30452368)
    • (2000) Biochemistry , vol.39 , Issue.27 , pp. 7943-7955
    • Vetting, M.W.1    D'Argenio, D.A.2    Ornston, L.N.3    Ohlendorf, D.H.4
  • 37
    • 1842762173 scopus 로고    scopus 로고
    • Understanding and improving NADPH-dependent reactions by nongrowing Escherichia coli cells
    • DOI 10.1021/bp030044m
    • AZ Walton JD Stewart 2004 Understanding and improving NADPH-dependent reactions by nongrowing Escherichia coli cells Biotechnol Prog 20 2 403 411 10.1021/bp030044m 1:CAS:528:DC%2BD3sXptlOhtLk%3D (Pubitemid 38463598)
    • (2004) Biotechnology Progress , vol.20 , Issue.2 , pp. 403-411
    • Walton, A.Z.1    Stewart, J.D.2


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