메뉴 건너뛰기




Volumn 3, Issue 1, 2010, Pages 48-58

Inter-conversion of catalytic abilities in a bifunctional carboxyl/feruloyl-esterase from earthworm gut metagenome

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENYL ESTER; ASPARAGINE; ASPARTIC ACID; CARBOXYLESTERASE; CINNAMATE ESTER; ESTER DERIVATIVE; ESTERASE; FERULOYL ESTERASE; HISTIDINE; LYSINE; PROTEIN 3A6; SERINE; UNCLASSIFIED DRUG;

EID: 77952891703     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/j.1751-7915.2009.00135.x     Document Type: Article
Times cited : (16)

References (29)
  • 1
    • 34250879694 scopus 로고    scopus 로고
    • The psychrophilic bacterium Pseudoalteromonas halosplanktis TAC125 possesses a gene coding for a cold-adapted feruloyl esterase activity that shares homology with esterase enzymes from gamma-proteobacteria and yeast
    • Aurilia, V., Parracino, A., Saviano, M., Rossi, M., and D'Auria, S. (2007) The psychrophilic bacterium Pseudoalteromonas halosplanktis TAC125 possesses a gene coding for a cold-adapted feruloyl esterase activity that shares homology with esterase enzymes from gamma-proteobacteria and yeast. Gene 397: 51-57.
    • (2007) Gene , vol.397 , pp. 51-57
    • Aurilia, V.1    Parracino, A.2    Saviano, M.3    Rossi, M.4    D'Auria, S.5
  • 2
    • 39249083636 scopus 로고    scopus 로고
    • Microbial carbohydrate esterases in cold adapted environments
    • Aurilia, V., Parracino, A., and D'Auria, S. (2008) Microbial carbohydrate esterases in cold adapted environments. Gene 410: 234-240.
    • (2008) Gene , vol.410 , pp. 234-240
    • Aurilia, V.1    Parracino, A.2    D'Auria, S.3
  • 3
    • 38649093655 scopus 로고    scopus 로고
    • Biotechnological applications and potential of fungal feruloyl esterases based on prevalence, classification and biochemical diversity
    • Benoit, I., Danchin, E.G., Bleichrodt, R.J., and de Vries, R.P. (2008) Biotechnological applications and potential of fungal feruloyl esterases based on prevalence, classification and biochemical diversity. Biotechnol Lett 30: 387-396.
    • (2008) Biotechnol Lett , vol.30 , pp. 387-396
    • Benoit, I.1    Danchin, E.G.2    Bleichrodt, R.J.3    de Vries, R.P.4
  • 5
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: Classification, properties and application in biocatalysis
    • Bornscheuer, U.T. (2002) Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol Rev 26: 73-81.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 73-81
    • Bornscheuer, U.T.1
  • 6
    • 1542269173 scopus 로고    scopus 로고
    • Functional classification of the microbial feruloyl esterases
    • Crepin, V.F., Faulds, C.B., and Connerton, I.F. (2004) Functional classification of the microbial feruloyl esterases. Appl Microbiol Biotechnol 63: 647-652.
    • (2004) Appl Microbiol Biotechnol , vol.63 , pp. 647-652
    • Crepin, V.F.1    Faulds, C.B.2    Connerton, I.F.3
  • 7
    • 24644517613 scopus 로고    scopus 로고
    • Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger
    • Faulds, C.B., Molina, R., Gonzalez, R., Husband, F., Juge, N., Sanz-Aparicio, J., and Hermoso, J.A. (2005) Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger. FEBS J 272: 4362-4371.
    • (2005) FEBS J , vol.272 , pp. 4362-4371
    • Faulds, C.B.1    Molina, R.2    Gonzalez, R.3    Husband, F.4    Juge, N.5    Sanz-Aparicio, J.6    Hermoso, J.A.7
  • 8
    • 36249002724 scopus 로고    scopus 로고
    • Feruloyl esterases as biotechnological tools: Current and future perspectives
    • Fazary, A.E., and Ju, Y.H. (2007) Feruloyl esterases as biotechnological tools: current and future perspectives. Acta Biochim Biophys Sin 39: 811-828.
    • (2007) Acta Biochim Biophys Sin , vol.39 , pp. 811-828
    • Fazary, A.E.1    Ju, Y.H.2
  • 9
    • 27544497498 scopus 로고    scopus 로고
    • Combination of computational pre-screening and experimental library construction can accelerate enzyme optimization by directed evolution
    • Funke, S.A., Otte, N., Eggert, T., Bocola, M., Jaeger, K.E., and Thiel, W. (2005) Combination of computational pre-screening and experimental library construction can accelerate enzyme optimization by directed evolution. Protein Eng Des Sel 18: 509-514.
    • (2005) Protein Eng Des Sel , vol.18 , pp. 509-514
    • Funke, S.A.1    Otte, N.2    Eggert, T.3    Bocola, M.4    Jaeger, K.E.5    Thiel, W.6
  • 10
    • 1842686201 scopus 로고    scopus 로고
    • The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family
    • Hermoso, J.A., Sanz-Aparicio, J., Molina, R., Juge, N., González, R., and Faulds, C.B. (2004) The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family. J Mol Biol 338: 495-506.
    • (2004) J Mol Biol , vol.338 , pp. 495-506
    • Hermoso, J.A.1    Sanz-Aparicio, J.2    Molina, R.3    Juge, N.4    González, R.5    Faulds, C.B.6
  • 11
    • 33947155728 scopus 로고    scopus 로고
    • Inverting enantioselectivity of Burkholderia gladioli esterase EstB by directed and designed evolution
    • Ivancic, M., Valinger, G., Gruber, K., and Schwab, H. (2007) Inverting enantioselectivity of Burkholderia gladioli esterase EstB by directed and designed evolution. J Biotechnol 129: 109-122.
    • (2007) J Biotechnol , vol.129 , pp. 109-122
    • Ivancic, M.1    Valinger, G.2    Gruber, K.3    Schwab, H.4
  • 12
    • 48749116260 scopus 로고    scopus 로고
    • Purification and characteristics of feruloyl esterase from Aspergillus awamori G-2 strain
    • Kanauchi, M., Watanabe, S., Tsukada, T., Atta, K., Kakuta, T., and Koizumi, T. (2008) Purification and characteristics of feruloyl esterase from Aspergillus awamori G-2 strain. J Food Sci 73: C458-463.
    • (2008) J Food Sci , vol.73
    • Kanauchi, M.1    Watanabe, S.2    Tsukada, T.3    Atta, K.4    Kakuta, T.5    Koizumi, T.6
  • 13
    • 14544295340 scopus 로고    scopus 로고
    • Mutational analysis of a feruloyl esterase from Aspergillus awamori involved in substrate discrimination and pH dependence
    • Koseki, T., Takahashi, K., Fushinobu, S., Lefuji, H., Iwano, K., Hasihuze, K., and Matsuzawa, H. (2005) Mutational analysis of a feruloyl esterase from Aspergillus awamori involved in substrate discrimination and pH dependence. Biochim Biophys Acta 1722: 200-208.
    • (2005) Biochim Biophys Acta , vol.1722 , pp. 200-208
    • Koseki, T.1    Takahashi, K.2    Fushinobu, S.3    Lefuji, H.4    Iwano, K.5    Hasihuze, K.6    Matsuzawa, H.7
  • 14
    • 67349198849 scopus 로고    scopus 로고
    • Characterization of two distinct feruloyl esterases, AoFaeB and AoFaeC, from Aspergillus oryzae
    • Koseki, T., Hori, A., Seki, S., Murayama, T., and Shiono, Y. (2009) Characterization of two distinct feruloyl esterases, AoFaeB and AoFaeC, from Aspergillus oryzae. Appl Microbiol Biotechnol 83: 689-696.
    • (2009) Appl Microbiol Biotechnol , vol.83 , pp. 689-696
    • Koseki, T.1    Hori, A.2    Seki, S.3    Murayama, T.4    Shiono, Y.5
  • 15
    • 33751414256 scopus 로고    scopus 로고
    • Tracking the connection between evolutionary and functional shifts using the fungal lipase/feruloyl esterase A family
    • Levasseur, A., Gouret, P., Lesage-Meessen, L., Asther, M., Record, E., and Pontarotti, P. (2006) Tracking the connection between evolutionary and functional shifts using the fungal lipase/feruloyl esterase A family. BMC Evol Biol 6: 92.
    • (2006) BMC Evol Biol , vol.6 , pp. 92
    • Levasseur, A.1    Gouret, P.2    Lesage-Meessen, L.3    Asther, M.4    Record, E.5    Pontarotti, P.6
  • 17
    • 0035813133 scopus 로고    scopus 로고
    • Residues at the active site of the esterase 2 from Alicyclobacillus acidocaldarius involved in substrate specificity and catalytic activity at high temperature
    • Manco, G., Mandrich, L., and Rossi, M. (2001) Residues at the active site of the esterase 2 from Alicyclobacillus acidocaldarius involved in substrate specificity and catalytic activity at high temperature. J Biol Chem 276: 37482-37490.
    • (2001) J Biol Chem , vol.276 , pp. 37482-37490
    • Manco, G.1    Mandrich, L.2    Rossi, M.3
  • 18
    • 33644984271 scopus 로고    scopus 로고
    • Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides
    • Mee-Hie Cho, C., Mulchandani, A., and Chen, W. (2006) Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides. Protein Eng Des Sel 19: 99-105.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 99-105
    • Mee-Hie Cho, C.1    Mulchandani, A.2    Chen, W.3
  • 19
    • 42549139751 scopus 로고    scopus 로고
    • Cloning, characterization and functional expression of an alkalitolerant type C feruloyl esterase from Fusarium oxysporum
    • Moukouli, M., Topakas, E., and Christakopoulous, P. (2008) Cloning, characterization and functional expression of an alkalitolerant type C feruloyl esterase from Fusarium oxysporum. Appl Microbiol Biotechnol 79: 245-254.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 245-254
    • Moukouli, M.1    Topakas, E.2    Christakopoulous, P.3
  • 20
    • 34548289533 scopus 로고    scopus 로고
    • Engineering of Pseudomonas aeruginosa lipase by directed evolution for enhanced amidase activity: Mechanistic implication for amide hydrolysis by serine hydrolases
    • Nakagawa, Y., Hasegawa, A., Hiratake, J., and Sakata, K. (2007) Engineering of Pseudomonas aeruginosa lipase by directed evolution for enhanced amidase activity: mechanistic implication for amide hydrolysis by serine hydrolases. Protein Eng Des Sel 20: 339-346.
    • (2007) Protein Eng Des Sel , vol.20 , pp. 339-346
    • Nakagawa, Y.1    Hasegawa, A.2    Hiratake, J.3    Sakata, K.4
  • 21
    • 0035195708 scopus 로고    scopus 로고
    • Contribution of Gln9 and Phe80 to substrate binding in ribonuclease MC1 from bitter gourd seeds
    • Numata, T., and Kimura, M. (2001) Contribution of Gln9 and Phe80 to substrate binding in ribonuclease MC1 from bitter gourd seeds. J Biochem 130: 621-626.
    • (2001) J Biochem , vol.130 , pp. 621-626
    • Numata, T.1    Kimura, M.2
  • 23
    • 33846152664 scopus 로고    scopus 로고
    • A type B feruloyl esterase from Aspergillus nidulans with broad pH applicability
    • Shin, H.D., and Chen, R.R. (2007) A type B feruloyl esterase from Aspergillus nidulans with broad pH applicability. Appl Microbiol Biotechnol 73: 1323-1330.
    • (2007) Appl Microbiol Biotechnol , vol.73 , pp. 1323-1330
    • Shin, H.D.1    Chen, R.R.2
  • 24
    • 21444453248 scopus 로고    scopus 로고
    • Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum
    • Tarbouriech, N., Prates, J.A.M., Fintes, C.M.G.A., and Davis, G.J. (2005) Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum. Acta Cryst 61: 194-197.
    • (2005) Acta Cryst , vol.61 , pp. 194-197
    • Tarbouriech, N.1    Prates, J.A.M.2    Fintes, C.M.G.A.3    Davis, G.J.4
  • 26
    • 33745826249 scopus 로고    scopus 로고
    • Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation
    • Wang, Q., Yang, G., Liu, Y., and Feng, Y. (2006) Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation. J Biol Chem 281: 18618-18625.
    • (2006) J Biol Chem , vol.281 , pp. 18618-18625
    • Wang, Q.1    Yang, G.2    Liu, Y.3    Feng, Y.4
  • 27
    • 16544386014 scopus 로고    scopus 로고
    • Purification and characterization of a feruloyl esterase from the intestinal bacterium Lactobacillus acidophilus
    • Wang, X., Geng, X., Egashira, Y., and Sanada, H. (2004) Purification and characterization of a feruloyl esterase from the intestinal bacterium Lactobacillus acidophilus. Appl Environ Microbiol 70: 2367-2372.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 2367-2372
    • Wang, X.1    Geng, X.2    Egashira, Y.3    Sanada, H.4
  • 28
  • 29
    • 33646874875 scopus 로고    scopus 로고
    • Feruloyl esterase: A key enzyme in biomass degradation
    • Wong, D.W. (2006) Feruloyl esterase: a key enzyme in biomass degradation. Appl Biochem Biotechnol 133: 87-112.
    • (2006) Appl Biochem Biotechnol , vol.133 , pp. 87-112
    • Wong, D.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.