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Volumn 168, Issue 3, 2013, Pages 264-270

Pushing the equilibrium of regio-complementary carboxylation of phenols and hydroxystyrene derivatives

Author keywords

Biotransformation; Carboxylation; Decarboxylase; Kolbe Schmitt reaction

Indexed keywords

BIOTRANSFORMATION; DECARBOXYLASES; ELECTRON-RICH AROMATICS; KOLBE-SCHMITT REACTION; NATURAL SUBSTRATES; REACTION CONDITIONS; REACTION TEMPERATURE; SUBSTRATE CONCENTRATIONS;

EID: 84887827426     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.07.017     Document Type: Article
Times cited : (30)

References (59)
  • 1
    • 0002889301 scopus 로고
    • Aspects of biocatalyst stability in organic solvents
    • Adlercreutz P., Mattiasson B. Aspects of biocatalyst stability in organic solvents. Biocata 1987, 1:99-108.
    • (1987) Biocata , vol.1 , pp. 99-108
    • Adlercreutz, P.1    Mattiasson, B.2
  • 3
    • 34547284071 scopus 로고    scopus 로고
    • 2 as a chemical feedstock: opportunities and challenges
    • 2 as a chemical feedstock: opportunities and challenges. Dalton Trans. 2007, 2975-2992.
    • (2007) Dalton Trans. , pp. 2975-2992
    • Aresta, M.1    Dibenedetto, A.2
  • 4
    • 27644582978 scopus 로고    scopus 로고
    • Unusual reactions involved in anaerobic metabolism of phenolic compounds
    • Boll M., Fuchs G. Unusual reactions involved in anaerobic metabolism of phenolic compounds. Biol. Chem. 2005, 386:989-997.
    • (2005) Biol. Chem. , vol.386 , pp. 989-997
    • Boll, M.1    Fuchs, G.2
  • 5
    • 37749049389 scopus 로고    scopus 로고
    • Cation and strong co-solute effects on protein kinetic stability
    • Broering J.M., Bommarius A.S. Cation and strong co-solute effects on protein kinetic stability. Biochem. Soc. Trans. 2007, 35:1602-1605. 10.1042/BST0351602.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1602-1605
    • Broering, J.M.1    Bommarius, A.S.2
  • 6
    • 54549120214 scopus 로고    scopus 로고
    • Kinetic model of salt-induced protein deactivation
    • Broering J.M., Bommarius A.S. Kinetic model of salt-induced protein deactivation. J. Phys. Chem. B 2008, 112:12768-12775.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 12768-12775
    • Broering, J.M.1    Bommarius, A.S.2
  • 7
    • 70350701157 scopus 로고    scopus 로고
    • Intensification of the capillary-based Kolbe Schmitt synthesis from resorcinol by reactive ionic liquids microwave heating, or a combination thereof
    • Benaskar F., Hessel V., Krtschil U., Löb P., Stark A. Intensification of the capillary-based Kolbe Schmitt synthesis from resorcinol by reactive ionic liquids microwave heating, or a combination thereof. Org. Process Res. Dev. 2009, 19:970-982.
    • (2009) Org. Process Res. Dev. , vol.19 , pp. 970-982
    • Benaskar, F.1    Hessel, V.2    Krtschil, U.3    Löb, P.4    Stark, A.5
  • 10
    • 78650251149 scopus 로고    scopus 로고
    • Chemistry of carbon dioxide relevant to its utilization: a personal perspective
    • Darensbourg D.J. Chemistry of carbon dioxide relevant to its utilization: a personal perspective. Inorg. Chem. 2010, 49:10765-10780.
    • (2010) Inorg. Chem. , vol.49 , pp. 10765-10780
    • Darensbourg, D.J.1
  • 11
    • 0028890051 scopus 로고
    • Purification and characterization of ferulate and p-coumarate decarboxylase from Bacillus pumilus
    • Degrassi G., Polverino de Laureto P., Bruschi C.V. Purification and characterization of ferulate and p-coumarate decarboxylase from Bacillus pumilus. Appl. Environ. Microbiol. 1995, 61:326-332.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 326-332
    • Degrassi, G.1    Polverino de Laureto, P.2    Bruschi, C.V.3
  • 13
    • 0026892825 scopus 로고
    • Designing enzymes for use in organic solvents
    • Dordick J.S. Designing enzymes for use in organic solvents. Biotechnol. Prog. 1992, 8:259-267.
    • (1992) Biotechnol. Prog. , vol.8 , pp. 259-267
    • Dordick, J.S.1
  • 14
    • 84863932391 scopus 로고    scopus 로고
    • Mutational analysis of phenolic acid decarboxylase from Bacillus subtilis (BsPAD), which converts bio-derived phenolic acids to styrene derivatives
    • Frank A., Eborall W., Hyde R., Hart S., Turkenburg J.P., Grogan G. Mutational analysis of phenolic acid decarboxylase from Bacillus subtilis (BsPAD), which converts bio-derived phenolic acids to styrene derivatives. Catal. Sci. Technol. 2012, 2:1568-1574.
    • (2012) Catal. Sci. Technol. , vol.2 , pp. 1568-1574
    • Frank, A.1    Eborall, W.2    Hyde, R.3    Hart, S.4    Turkenburg, J.P.5    Grogan, G.6
  • 16
    • 33845923659 scopus 로고    scopus 로고
    • Crystal structures of nonoxidative zinc-dependent 2,6-dihydroxybenzoate (γ-resorcylate) decarboxylase from Rhizobium sp. strain MTP-10005
    • Goto M., Hayashi H., Miyahara I., Hirotsu K., Yoshida M., Oikawa T. Crystal structures of nonoxidative zinc-dependent 2,6-dihydroxybenzoate (γ-resorcylate) decarboxylase from Rhizobium sp. strain MTP-10005. J. Biol. Chem. 2006, 281:34365-34373.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34365-34373
    • Goto, M.1    Hayashi, H.2    Miyahara, I.3    Hirotsu, K.4    Yoshida, M.5    Oikawa, T.6
  • 17
    • 79952574595 scopus 로고    scopus 로고
    • Cloning, sequencing, and overexpression in Escherichia coli of the Enterobacter sp. Px6-4 gene for ferulic acid decarboxylases
    • Gu W., Li X., Huang J., Duan Y., Meng Z., Zhang K.-Q., Yang J. Cloning, sequencing, and overexpression in Escherichia coli of the Enterobacter sp. Px6-4 gene for ferulic acid decarboxylases. Appl. Microbiol. Biotechnol. 2010, 89:1797-1805.
    • (2010) Appl. Microbiol. Biotechnol. , vol.89 , pp. 1797-1805
    • Gu, W.1    Li, X.2    Huang, J.3    Duan, Y.4    Meng, Z.5    Zhang, K.-Q.6    Yang, J.7
  • 18
    • 79251633326 scopus 로고    scopus 로고
    • Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp. Px6-4
    • doi:10.1371/journal.pone.0016262
    • Gu W., Yang J., Lou Z., Liang L., Sun Y., Huang J., Li X., Cao Y., Meng Z., Zhang K.-Q. Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp. Px6-4. PLoS ONE 2011, 6:e16262. doi:10.1371/journal.pone.0016262.
    • (2011) PLoS ONE , vol.6
    • Gu, W.1    Yang, J.2    Lou, Z.3    Liang, L.4    Sun, Y.5    Huang, J.6    Li, X.7    Cao, Y.8    Meng, Z.9    Zhang, K.-Q.10
  • 19
    • 0028396938 scopus 로고
    • Thermodynamic predictions for biocatalysis in nonconventional media: theory, tests, and recommendations for experimental design and analysis
    • Halling P.J. Thermodynamic predictions for biocatalysis in nonconventional media: theory, tests, and recommendations for experimental design and analysis. Enzyme Microb. Technol. 1994, 16:178-206.
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 178-206
    • Halling, P.J.1
  • 20
    • 0028952872 scopus 로고
    • Purification and characterization of an oxygen-sensitive reversible 4-hydroxybenzoate decarboxylase from Clostridium hydroxybenzoicium
    • He.Z., Wiegel J. Purification and characterization of an oxygen-sensitive reversible 4-hydroxybenzoate decarboxylase from Clostridium hydroxybenzoicium. Eur. J. Biochem. 1995, 229:77-82.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 77-82
    • He, Z.1    Wiegel, J.2
  • 21
    • 0029891655 scopus 로고    scopus 로고
    • Purification and characterization of an oxygen-sensitive, reversible 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicium
    • He Z., Wiegel J. Purification and characterization of an oxygen-sensitive, reversible 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicium. J. Bacteriol. 1996, 178:3539-3543.
    • (1996) J. Bacteriol. , vol.178 , pp. 3539-3543
    • He, Z.1    Wiegel, J.2
  • 23
    • 79954627461 scopus 로고    scopus 로고
    • Transition-metal-catalyzed C-C bond formation through the fixation of carbon dioxide
    • Huang K., Sun C.-L., Shi Z.-J. Transition-metal-catalyzed C-C bond formation through the fixation of carbon dioxide. Chem. Soc. Rev. 2011, 40:2435-2452.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 2435-2452
    • Huang, K.1    Sun, C.-L.2    Shi, Z.-J.3
  • 24
    • 5144220809 scopus 로고    scopus 로고
    • Reversible and nonoxidative γ-resorcylic acid decarboxylases: characterization and gene cloning of a novel enzyme catalyzing carboxylation of resorcinol, 1,3-dihydroxybenzene, from Rhizobium radiobacter
    • Ishii Y., Narimatsu Y., Iwasaki Y., Arai N., Kino K., Kirimura K. Reversible and nonoxidative γ-resorcylic acid decarboxylases: characterization and gene cloning of a novel enzyme catalyzing carboxylation of resorcinol, 1,3-dihydroxybenzene, from Rhizobium radiobacter. Biochem. Biophys. Res. Commun. 2004, 324:611-620.
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 611-620
    • Ishii, Y.1    Narimatsu, Y.2    Iwasaki, Y.3    Arai, N.4    Kino, K.5    Kirimura, K.6
  • 25
    • 34147151230 scopus 로고    scopus 로고
    • Regioselective and enzymatic production of (-resorcylic acid from resorcinol using recombinant Escherichia coli cells expressing a novel decarboxylase gene
    • Iwasaki Y., Kino K., Nishide H., Kirimura K. Regioselective and enzymatic production of (-resorcylic acid from resorcinol using recombinant Escherichia coli cells expressing a novel decarboxylase gene. Biotechnol. Lett. 2007, 29:819-822.
    • (2007) Biotechnol. Lett. , vol.29 , pp. 819-822
    • Iwasaki, Y.1    Kino, K.2    Nishide, H.3    Kirimura, K.4
  • 26
    • 0000743390 scopus 로고
    • Viscosity B-coefficients of ions in solutions
    • Jenkins H.D.B., Marcus Y. Viscosity B-coefficients of ions in solutions. Chem. Rev. 1995, 95:2695-2724.
    • (1995) Chem. Rev. , vol.95 , pp. 2695-2724
    • Jenkins, H.D.B.1    Marcus, Y.2
  • 27
    • 84874376569 scopus 로고    scopus 로고
    • Bioconversion of p-coumaric acid to p-hydroxystyrene using phenolic acid decarboxylases from B. amyloliquefaciens in biphasic reaction system
    • Jung D.-H., Choi W., Choi K.-Y., Jung E., Yun H., Kazlauskas R.J., Kim B.-G. Bioconversion of p-coumaric acid to p-hydroxystyrene using phenolic acid decarboxylases from B. amyloliquefaciens in biphasic reaction system. Appl. Microbiol. Biotechnol. 2013.
    • (2013) Appl. Microbiol. Biotechnol.
    • Jung, D.-H.1    Choi, W.2    Choi, K.-Y.3    Jung, E.4    Yun, H.5    Kazlauskas, R.J.6    Kim, B.-G.7
  • 28
    • 77950228892 scopus 로고    scopus 로고
    • Enzymatic Kolbe-Schmitt reaction to form salicylic acid from phenol: enzymatic characterization and gene identification of a novel enyzme, Trichosporon moniliiforme salicylic acid decarboxylase
    • Kirimura K., Gunji H., Wakayama R., Hattori T., Ishii Y. Enzymatic Kolbe-Schmitt reaction to form salicylic acid from phenol: enzymatic characterization and gene identification of a novel enyzme, Trichosporon moniliiforme salicylic acid decarboxylase. Biochem. Biophys. Res. Commun. 2010, 394:279-284.
    • (2010) Biochem. Biophys. Res. Commun. , vol.394 , pp. 279-284
    • Kirimura, K.1    Gunji, H.2    Wakayama, R.3    Hattori, T.4    Ishii, Y.5
  • 29
    • 79551484569 scopus 로고    scopus 로고
    • Production of p-aminosalicylic acid through enzymatic Kolbe-Schmitt reaction catalyzed by reversible salicylic acid decarboxylase
    • Kirimura K., Yanaso S., Kosaka S., Koyama K., Hattori T., Ishii Y. Production of p-aminosalicylic acid through enzymatic Kolbe-Schmitt reaction catalyzed by reversible salicylic acid decarboxylase. Chem. Lett. 2011, 40:206-208.
    • (2011) Chem. Lett. , vol.40 , pp. 206-208
    • Kirimura, K.1    Yanaso, S.2    Kosaka, S.3    Koyama, K.4    Hattori, T.5    Ishii, Y.6
  • 31
    • 71049144816 scopus 로고    scopus 로고
    • Flow chemistry of the Kolbe-Schmitt synthesis from resorcinol: process intensification by alternative solvents, new reagents and advanced reactor engineering
    • Krtschil U., Hessel V., Reinhard D., Stark A. Flow chemistry of the Kolbe-Schmitt synthesis from resorcinol: process intensification by alternative solvents, new reagents and advanced reactor engineering. Chem. Eng. Technol. 2009, 32:1774-1789.
    • (2009) Chem. Eng. Technol. , vol.32 , pp. 1774-1789
    • Krtschil, U.1    Hessel, V.2    Reinhard, D.3    Stark, A.4
  • 32
    • 0028360990 scopus 로고
    • Some aspects of biocatalysis in organic solvents
    • Kvittingen L. Some aspects of biocatalysis in organic solvents. Tetrahedron 1994, 50:8253-8274.
    • (1994) Tetrahedron , vol.50 , pp. 8253-8274
    • Kvittingen, L.1
  • 33
    • 33947461091 scopus 로고
    • The Kolbe-Schmitt reaction
    • Lindsey A.S., Feskey H. The Kolbe-Schmitt reaction. Chem. Rev. 1957, 57:583-620.
    • (1957) Chem. Rev. , vol.57 , pp. 583-620
    • Lindsey, A.S.1    Feskey, H.2
  • 34
    • 33846296643 scopus 로고    scopus 로고
    • Purification and characterization of a 4-hydroxybenzoate decarboxylases from Chlamydophila pneumoniae
    • Liu J., Zhang X., Zhou S., Tao P., Liu L. Purification and characterization of a 4-hydroxybenzoate decarboxylases from Chlamydophila pneumoniae. Curr. Microbiol. 2007, 54:102-107.
    • (2007) Curr. Microbiol. , vol.54 , pp. 102-107
    • Liu, J.1    Zhang, X.2    Zhou, S.3    Tao, P.4    Liu, L.5
  • 35
    • 39749148299 scopus 로고    scopus 로고
    • Properties of the reversible nonoxidative vanillate/4-hydroxybenzoate decarboxylases from Bacillus subtilis
    • Lupa B., Lyon D., Shaw L.N., Sieprawska-Lupa M., Wiegel J. Properties of the reversible nonoxidative vanillate/4-hydroxybenzoate decarboxylases from Bacillus subtilis. Can. J. Microbiol. 2008, 54:75-81.
    • (2008) Can. J. Microbiol. , vol.54 , pp. 75-81
    • Lupa, B.1    Lyon, D.2    Shaw, L.N.3    Sieprawska-Lupa, M.4    Wiegel, J.5
  • 36
    • 33745863484 scopus 로고    scopus 로고
    • Purification, characterization, and gene cloning of 4-hydroxybenzoate decarboxylase of Enterobacter cloacae P240
    • Matsui T., Yoshida T., Hayashi T., Nagasawa T. Purification, characterization, and gene cloning of 4-hydroxybenzoate decarboxylase of Enterobacter cloacae P240. Arch. Microbiol. 2006, 186:21-29. 10.1007/s00203-006-0117-5.
    • (2006) Arch. Microbiol. , vol.186 , pp. 21-29
    • Matsui, T.1    Yoshida, T.2    Hayashi, T.3    Nagasawa, T.4
  • 37
    • 33750288577 scopus 로고    scopus 로고
    • Regioselective carboxylation of 1,3-dihydroxybenzene by 2,6-dihydroxybenzoate decarboxylase of Pandoraea sp. 12B-2
    • Matsui T., Yoshida T., Yoshimura T., Nagasawa T. Regioselective carboxylation of 1,3-dihydroxybenzene by 2,6-dihydroxybenzoate decarboxylase of Pandoraea sp. 12B-2. Appl. Microbiol. Biotechnol. 2006, 73:95-102.
    • (2006) Appl. Microbiol. Biotechnol. , vol.73 , pp. 95-102
    • Matsui, T.1    Yoshida, T.2    Yoshimura, T.3    Nagasawa, T.4
  • 38
    • 78149335955 scopus 로고    scopus 로고
    • Structural analysis of Bacillus pumilus phenolic acid decarboxylase, a lipocalin-fold enzyme
    • Matte A., Grosse S., Bergeron H., Abokitse K., Lau P.C.K. Structural analysis of Bacillus pumilus phenolic acid decarboxylase, a lipocalin-fold enzyme. Acta Cryst. Sect. F 2010, 66:1407-1414.
    • (2010) Acta Cryst. Sect. F , vol.66 , pp. 1407-1414
    • Matte, A.1    Grosse, S.2    Bergeron, H.3    Abokitse, K.4    Lau, P.C.K.5
  • 39
    • 0041931993 scopus 로고    scopus 로고
    • Biocatalysis in ionic liquids - advantages beyond green technology
    • Park S., Kazlauskas R.J. Biocatalysis in ionic liquids - advantages beyond green technology. Curr. Opin. Biotechnol. 2003, 14:432-437.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 432-437
    • Park, S.1    Kazlauskas, R.J.2
  • 40
    • 75849149895 scopus 로고    scopus 로고
    • Environmental fate and toxicity of ionic liquids: a review
    • Pham T.P.T., Cho C.-W., Yun Y.-S. Environmental fate and toxicity of ionic liquids: a review. Water Res. 2010, 44:352-372.
    • (2010) Water Res. , vol.44 , pp. 352-372
    • Pham, T.P.T.1    Cho, C.-W.2    Yun, Y.-S.3
  • 41
    • 80052952886 scopus 로고    scopus 로고
    • Carbon dioxide recycling: emergine large-scale technologies with industrial potential
    • Quadrelli E.A., Centi G., Duplan J.-L., Perathoner S. Carbon dioxide recycling: emergine large-scale technologies with industrial potential. ChemSusChem 2011, 4:1194-1215.
    • (2011) ChemSusChem , vol.4 , pp. 1194-1215
    • Quadrelli, E.A.1    Centi, G.2    Duplan, J.-L.3    Perathoner, S.4
  • 42
    • 77951242130 scopus 로고    scopus 로고
    • P-Coumaric acid decarboxylase from Lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism
    • Rodriguez H., Angulo I., de las Rivas B., Campillo N., Paez J.A., Munoz R., Mancheno J.M. p-Coumaric acid decarboxylase from Lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism. Proteins 2010, 78:1662-1676.
    • (2010) Proteins , vol.78 , pp. 1662-1676
    • Rodriguez, H.1    Angulo, I.2    de las Rivas, B.3    Campillo, N.4    Paez, J.A.5    Munoz, R.6    Mancheno, J.M.7
  • 43
    • 34447102805 scopus 로고    scopus 로고
    • Tansformation of carbon dioxide
    • Sakakura T., Choi J.-C., Yasuda H. Tansformation of carbon dioxide. Chem. Rev. 2007, 107:2365-2387.
    • (2007) Chem. Rev. , vol.107 , pp. 2365-2387
    • Sakakura, T.1    Choi, J.-C.2    Yasuda, H.3
  • 44
    • 3042857782 scopus 로고    scopus 로고
    • Phenylphosphate Carboxylase: a new C-C lyase involved in anaerobic phenol metabolism in Thauera aromatica
    • Schühle K., Fuchs G. Phenylphosphate Carboxylase: a new C-C lyase involved in anaerobic phenol metabolism in Thauera aromatica. J. Bacteriol. 2004, 186:4556-4567.
    • (2004) J. Bacteriol. , vol.186 , pp. 4556-4567
    • Schühle, K.1    Fuchs, G.2
  • 46
    • 84866358212 scopus 로고    scopus 로고
    • Carbon dioxide as a carbon source in organic transformation: carboncarbon bond forming reactions by transition-metal catalysts
    • Tsuji Y., Fujihara T. Carbon dioxide as a carbon source in organic transformation: carboncarbon bond forming reactions by transition-metal catalysts. Chem. Commun. 2012, 48:9956-9964.
    • (2012) Chem. Commun. , vol.48 , pp. 9956-9964
    • Tsuji, Y.1    Fujihara, T.2
  • 48
    • 0032532798 scopus 로고    scopus 로고
    • Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylases from Bacillus megaterium PYR2910
    • Wieser M., Fujii N., Yoshida T., Nagasawa T. Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylases from Bacillus megaterium PYR2910. Eur. J. Biochem. 1998, 257:495-499.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 495-499
    • Wieser, M.1    Fujii, N.2    Yoshida, T.3    Nagasawa, T.4
  • 49
    • 0032507911 scopus 로고    scopus 로고
    • Microbial synthesis of pyrrol-2-carboxylate by Bacillus megaterium PYR2910
    • Wieser M., Yoshida T., Nagasawa T. Microbial synthesis of pyrrol-2-carboxylate by Bacillus megaterium PYR2910. Tetrahedron Lett. 1998, 39:4309-4310.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 4309-4310
    • Wieser, M.1    Yoshida, T.2    Nagasawa, T.3
  • 50
    • 0035931382 scopus 로고    scopus 로고
    • Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase and its application
    • Wieser M., Yoshida T., Nagasawa T. Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase and its application. J. Mol. Catal. B: Enzym. 2001, 11:179-184.
    • (2001) J. Mol. Catal. B: Enzym. , vol.11 , pp. 179-184
    • Wieser, M.1    Yoshida, T.2    Nagasawa, T.3
  • 51
    • 84860170211 scopus 로고    scopus 로고
    • Regioselective enzymatic carboxylation of phenols and hydroxystyrene derivatives
    • Wuensch C., Glueck S.M., Gross J., Koszelewski D., Schober M., Faber K. Regioselective enzymatic carboxylation of phenols and hydroxystyrene derivatives. Org. Lett. 2012, 14:1974-1977.
    • (2012) Org. Lett. , vol.14 , pp. 1974-1977
    • Wuensch, C.1    Glueck, S.M.2    Gross, J.3    Koszelewski, D.4    Schober, M.5    Faber, K.6
  • 54
    • 0034034693 scopus 로고    scopus 로고
    • Enzymatic functionalization of aromatic N-heterocycles: hydroxylation and carboxylatiom
    • Yoshida T., Nagasawa T. Enzymatic functionalization of aromatic N-heterocycles: hydroxylation and carboxylatiom. J. Biosci. Bioeng. 2000, 89:111-118.
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 111-118
    • Yoshida, T.1    Nagasawa, T.2
  • 55
    • 0041334956 scopus 로고    scopus 로고
    • Novel reversible indole-3-carboxylate decarboxylase catalyzing nonoxidative decarboxylation
    • Yoshida T., Fujita K., Nagasawa T. Novel reversible indole-3-carboxylate decarboxylase catalyzing nonoxidative decarboxylation. Biosci. Biotechnol. Biochem. 2002, 66:2388-2394.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 2388-2394
    • Yoshida, T.1    Fujita, K.2    Nagasawa, T.3
  • 56
    • 4944251045 scopus 로고    scopus 로고
    • Thermophilic, reversible (-resorcylate decarboxylase from Rhizobium sp. strain MTP-10005: purification, molecular characterization, and expression
    • Yoshida M., Fukuhara N., Oikawa T. Thermophilic, reversible (-resorcylate decarboxylase from Rhizobium sp. strain MTP-10005: purification, molecular characterization, and expression. J. Bacteriol. 2004, 186:6855-6863.
    • (2004) J. Bacteriol. , vol.186 , pp. 6855-6863
    • Yoshida, M.1    Fukuhara, N.2    Oikawa, T.3
  • 57
    • 3142619239 scopus 로고    scopus 로고
    • Purification and characterization of 2,6-dihydroxybenzoate decarboxylase reversibly catalyzing nonoxidative decarboxylation
    • Yoshida T., Hayakawa Y., Matsui T., Nagasawa T. Purification and characterization of 2,6-dihydroxybenzoate decarboxylase reversibly catalyzing nonoxidative decarboxylation. Arch. Microbiol. 2004, 181:391-397.
    • (2004) Arch. Microbiol. , vol.181 , pp. 391-397
    • Yoshida, T.1    Hayakawa, Y.2    Matsui, T.3    Nagasawa, T.4
  • 58
    • 77952243715 scopus 로고    scopus 로고
    • Regioselective carboxylation of catechol by 3,4-dihydroxybenzoate decarboxylase of Enterobacter cloacae P
    • Yoshida T., Inami Y., Matsui T., Nagasawa T. Regioselective carboxylation of catechol by 3,4-dihydroxybenzoate decarboxylase of Enterobacter cloacae P. Biotechnol. Lett. 2010, 32:701-705.
    • (2010) Biotechnol. Lett. , vol.32 , pp. 701-705
    • Yoshida, T.1    Inami, Y.2    Matsui, T.3    Nagasawa, T.4


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