메뉴 건너뛰기




Volumn 146, Issue 6, 2000, Pages 1391-1397

Three multidomain esterases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that carry divergent dockerin sequences

Author keywords

Cellulosome; Dockerin; Esterase; Rumen; Ruminococcus

Indexed keywords

ACETYLESTERASE; BACTERIAL ENZYME; ESTERASE; FERULIC ACID; GENE PRODUCT; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 0034080081     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-146-6-1391     Document Type: Article
Times cited : (76)

References (40)
  • 1
    • 0027498956 scopus 로고
    • p-Coumaroyl and feruloyl arabinoxylans from plant cell walls as substrates for ruminal bacteria
    • Akin, D. E., Borneman, W. S., Rigsby, L. L. & Martin, S. A. (1993). p-Coumaroyl and feruloyl arabinoxylans from plant cell walls as substrates for ruminal bacteria. Appl Environ Microbiol 59, 644-647.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 644-647
    • Akin, D.E.1    Borneman, W.S.2    Rigsby, L.L.3    Martin, S.A.4
  • 2
    • 0031033383 scopus 로고    scopus 로고
    • An Aspergillus niger esterase (FAE-III) and a recombinant Pseudomonas fluorescens subsp. Cellulosa esterase (XYLD) release 5,5′-ferulic dehydroodimer ('diferulic acid') from barley and wheat cell walls
    • Bartolomé, B., Faulds, C. B., Kroon, P. A., Waldron, K., Gilbert, H. J., Hazlewood, G. P. & Williamson, G. (1997). An Aspergillus niger esterase (FAE-III) and a recombinant Pseudomonas fluorescens subsp. cellulosa esterase (XYLD) release 5,5′-ferulic dehydroodimer ('diferulic acid') from barley and wheat cell walls. Appl Environ Microbiol 63, 208-212.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 208-212
    • Bartolomé, B.1    Faulds, C.B.2    Kroon, P.A.3    Waldron, K.4    Gilbert, H.J.5    Hazlewood, G.P.6    Williamson, G.7
  • 3
    • 0002540541 scopus 로고    scopus 로고
    • Cellulosome structure: Four-pronged attack using biochemistry, molecular biology, crystallography and bioinformatics
    • Edited by M. Claeyssens, W. Nerinckx & K. Piens. Cambridge: Royal Society of Chemistry
    • Bayer, E. A., Morag, E., Lamed, R., Yaron, S. & Shoham, Y. (1998a). Cellulosome structure: four-pronged attack using biochemistry, molecular biology, crystallography and bioinformatics. In Carbohydrases from Trichoderma reesei and Other Microorganisms, pp. 39-65. Edited by M. Claeyssens, W. Nerinckx & K. Piens. Cambridge: Royal Society of Chemistry.
    • (1998) Carbohydrases from Trichoderma Reesei and Other Microorganisms , pp. 39-65
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3    Yaron, S.4    Shoham, Y.5
  • 5
    • 0023029475 scopus 로고
    • Cooperativity of esterases and xylanases in enzymatic degradation of acetylxylan
    • Biely, P., MacKenzie, C. R., Puls, J. & Schneider, H. (1986). Cooperativity of esterases and xylanases in enzymatic degradation of acetylxylan. Bio/Technology 4, 731-733.
    • (1986) Bio/Technology , vol.4 , pp. 731-733
    • Biely, P.1    Mackenzie, C.R.2    Puls, J.3    Schneider, H.4
  • 6
    • 0041295729 scopus 로고    scopus 로고
    • Phenolic acid esterase activity of Clostridium thermocellum cellulosome is attributed to previously unknown domains of XynY and XynZ
    • (MIE Bioforum 98), Edited by K. Ohmiya, K. Hayashi, K. Sakka, Y. Kobayashi, S. Karita & T. Kimura. Tokyo: UNI Publishers
    • Blum, D. L., Kataeva, I., Li., X.-L. & Ljungdahl, L. G. (1998). Phenolic acid esterase activity of Clostridium thermocellum cellulosome is attributed to previously unknown domains of XynY and XynZ. In Genetics, Biochemistry and Ecology of Cellulose Degradation (MIE Bioforum 98), p. 478. Edited by K. Ohmiya, K. Hayashi, K. Sakka, Y. Kobayashi, S. Karita & T. Kimura. Tokyo: UNI Publishers.
    • (1998) Genetics, Biochemistry and Ecology of Cellulose Degradation , pp. 478
    • Blum, D.L.1    Kataeva, I.2    Li, X.-L.3    Ljungdahl, L.G.4
  • 7
    • 0025813571 scopus 로고
    • Isolation and characterization of p-coumaroyl esrerase from the anaerobic fungus Neocallimastix strain MC-2
    • Borneman, W. S., Ljungdahl, L. G., Hartley, R. D. & Akin, D. E. (1991). Isolation and characterization of p-coumaroyl esrerase from the anaerobic fungus Neocallimastix strain MC-2. Appl Environ Microbiol 57, 2337-2344.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 2337-2344
    • Borneman, W.S.1    Ljungdahl, L.G.2    Hartley, R.D.3    Akin, D.E.4
  • 8
    • 0026448264 scopus 로고
    • Purification and partial characterisation of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC2
    • Borneman, W. S., Ljungdahl, L. G., Hartley, R. D. & Akin, D. E. (1992). Purification and partial characterisation of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC2. Appl Environ Microbiol 58, 3762-3766.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3762-3766
    • Borneman, W.S.1    Ljungdahl, L.G.2    Hartley, R.D.3    Akin, D.E.4
  • 9
    • 0027611199 scopus 로고
    • Esterases of xylan degrading microorganisms: Production, properties and significance
    • Christov, L. P. & Prior, B. A. (1993). Esterases of xylan degrading microorganisms: production, properties and significance. Enzyme Microb Technol 15, 460-475.
    • (1993) Enzyme Microb Technol , vol.15 , pp. 460-475
    • Christov, L.P.1    Prior, B.A.2
  • 10
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins
    • Cygler, M., Schrag, J. D., Sussman, J. L. Harel, M., Silman, I., Gentry, M. K. & Doctor, B. P. (1993). Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Sci 2, 366-382.
    • (1993) Protein Sci , vol.2 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Doctor, B.P.7
  • 11
    • 0030272514 scopus 로고    scopus 로고
    • Cloning of a gene encoding cinnamoyl ester hydrolase from the ruminal bacterium Butyrivibrio fibrisolvens E14 by a novel method
    • Dalrymple, B. P., Swadling, Y., Cybinski, D. H. & Xue, G.-P. (1996). Cloning of a gene encoding cinnamoyl ester hydrolase from the ruminal bacterium Butyrivibrio fibrisolvens E14 by a novel method. FEMS Microbiol Lett 143, 115-120.
    • (1996) FEMS Microbiol Lett , vol.143 , pp. 115-120
    • Dalrymple, B.P.1    Swadling, Y.2    Cybinski, D.H.3    Xue, G.-P.4
  • 12
    • 0030864850 scopus 로고    scopus 로고
    • Three Neocallimastix patriciarum esterases associated with the degradation of complex polysaccharides are members of a new family of hydrolases
    • Dalrymple, B. P., Cybinski, D. H., Layton, I., McSweeney, C. S., Xue, G.-P., Swadling, Y. J. & Lowry, J. B. (1997). Three Neocallimastix patriciarum esterases associated with the degradation of complex polysaccharides are members of a new family of hydrolases. Microbiology 143, 2605-2614.
    • (1997) Microbiology , vol.143 , pp. 2605-2614
    • Dalrymple, B.P.1    Cybinski, D.H.2    Layton, I.3    McSweeney, C.S.4    Xue, G.-P.5    Swadling, Y.J.6    Lowry, J.B.7
  • 14
    • 0027231373 scopus 로고
    • A bifunctional enzyme, with separate xylanase and β(1,3-1,4)glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens
    • Flint, H. J., Martin, J. & McPherson, G. A. (1993). A bifunctional enzyme, with separate xylanase and β(1,3-1,4)glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens. J Bacteriol 175, 2943-2951.
    • (1993) J Bacteriol , vol.175 , pp. 2943-2951
    • Flint, H.J.1    Martin, J.2    McPherson, G.A.3
  • 15
    • 0027285934 scopus 로고
    • Sequencing of a Clostridium thermocellum gene cipA encoding the cellulosomal SL protein reveals an unusual degree of internal homology
    • Gerngross, V. T. & Demain, A. L. (1993). Sequencing of a Clostridium thermocellum gene cipA encoding the cellulosomal SL protein reveals an unusual degree of internal homology. Mol Microbiol 8, 325-334.
    • (1993) Mol Microbiol , vol.8 , pp. 325-334
    • Gerngross, V.T.1    Demain, A.L.2
  • 16
    • 0042798483 scopus 로고    scopus 로고
    • Hydrolysis and degradation of esterified phenolic acids from the maize cell wall by rumen microbial species
    • Giraud, I., Besle, J. M. & Fonty, G. (1997). Hydrolysis and degradation of esterified phenolic acids from the maize cell wall by rumen microbial species. Reprod Nutr Dev Suppl 52-53.
    • (1997) Reprod Nutr Dev Suppl , pp. 52-53
    • Giraud, I.1    Besle, J.M.2    Fonty, G.3
  • 17
    • 0024095009 scopus 로고
    • Nucleotide sequence and deletion analysis of the xylanase gene (xynZ) of Clostridium thermocellum
    • Grépinet, O., Chebrou, M.-C. & Béguin, P. (1988). Nucleotide sequence and deletion analysis of the xylanase gene (xynZ) of Clostridium thermocellum. J Bacteriol 170, 4582-4588.
    • (1988) J Bacteriol , vol.170 , pp. 4582-4588
    • Grépinet, O.1    Chebrou, M.-C.2    Béguin, P.3
  • 18
    • 0023773371 scopus 로고
    • Esrerase activities in Butyrivibrio fibrisolvens
    • Hespell, R. B. & O'Bryan-Shah, P. J. (1988). Esrerase activities in Butyrivibrio fibrisolvens. Appl Environ Microbiol 54, 1917-1927.
    • (1988) Appl Environ Microbiol , vol.54 , pp. 1917-1927
    • Hespell, R.B.1    O'Bryan-Shah, P.J.2
  • 19
    • 0028050797 scopus 로고
    • Covalent cross-links in the cell wall
    • Iiyama, K., Lam, T. P. T. & Stone, B. A. (1994). Covalent cross-links in the cell wall. Plant Physiol 104, 315-320.
    • (1994) Plant Physiol , vol.104 , pp. 315-320
    • Iiyama, K.1    Lam, T.P.T.2    Stone, B.A.3
  • 20
    • 0000090628 scopus 로고
    • Measurement of acetyl xylan esterase in Streptomyces
    • Johnson, K. G., Fontana, J. D. & MacKenzie, C. R. (1988). Measurement of acetyl xylan esterase in Streptomyces. Methods Enzymol 160, 552-560.
    • (1988) Methods Enzymol , vol.160 , pp. 552-560
    • Johnson, K.G.1    Fontana, J.D.2    Mackenzie, C.R.3
  • 22
    • 0030937055 scopus 로고    scopus 로고
    • Dockerin-like sequences from the rumen cellulolytic bacterium Ruminococcus flavefaciens
    • Kirby, J., Martin, J. C., Daniel, A. S. & Flint, H. J. (1997). Dockerin-like sequences from the rumen cellulolytic bacterium Ruminococcus flavefaciens. FEMS Microbiol Lett 149, 213-219.
    • (1997) FEMS Microbiol Lett , vol.149 , pp. 213-219
    • Kirby, J.1    Martin, J.C.2    Daniel, A.S.3    Flint, H.J.4
  • 23
    • 17744414050 scopus 로고    scopus 로고
    • Plant cell wall degrading enzyme complexes from the cellulolytic rumen bacterium Ruminococcus flavefaciens
    • Kirby, J., Aurilia, V., McCrae, S. I., Martin, J. C. & Flint, H. J. (1998). Plant cell wall degrading enzyme complexes from the cellulolytic rumen bacterium Ruminococcus flavefaciens. Biochem Soc Trans 26, S169.
    • (1998) Biochem Soc Trans , vol.26
    • Kirby, J.1    Aurilia, V.2    McCrae, S.I.3    Martin, J.C.4    Flint, H.J.5
  • 24
    • 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
  • 26
    • 0017736277 scopus 로고
    • Carbohydrate determination with 4-hydroxy-benzoic acid hydrazide (PAHBAH): Effect of bismuth on the reaction
    • Lever, M. (1977). Carbohydrate determination with 4-hydroxy-benzoic acid hydrazide (PAHBAH): effect of bismuth on the reaction. Anal Biochem 81, 21-27.
    • (1977) Anal Biochem , vol.81 , pp. 21-27
    • Lever, M.1
  • 28
    • 0343229549 scopus 로고    scopus 로고
    • Species specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: Prediction of specificity determinants of the dockerin domain
    • Pages, S., Belaich, A., Belaich, J.-P., Morag, E., Lamed, R., Shoham, Y. & Bayer, E. A. (1997). Species specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain. Proteins Struct Funct Genet 29, 517-527.
    • (1997) Proteins Struct Funct Genet , vol.29 , pp. 517-527
    • Pages, S.1    Belaich, A.2    Belaich, J.-P.3    Morag, E.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7
  • 29
    • 0002858834 scopus 로고
    • Sugar beer pectins: Chemical structure and gelation through oxidative coupling. Chemistry and function of pectins
    • Rombouts, F. M. & Thibault, J. F. (1986). Sugar beer pectins: chemical structure and gelation through oxidative coupling. Chemistry and function of pectins. ACS (Am Chem Soc) Symp Ser 310, 49-60.
    • (1986) ACS (Am Chem Soc) Symp Ser , vol.310 , pp. 49-60
    • Rombouts, F.M.1    Thibault, J.F.2
  • 30
    • 0028225196 scopus 로고
    • Recognition specificity of the duplicated segments present in Clostridium thermocellum endoglucanase CelD and in the cellulosome integrating protein CipA
    • Salamitou, S., Raynaud, O., Lemaire, M., Coughton, M., Béguin, P. & Aubert, J. P. (1994). Recognition specificity of the duplicated segments present in Clostridium thermocellum endoglucanase CelD and in the cellulosome integrating protein CipA. J Bacteriol 176, 2822-2827.
    • (1994) J Bacteriol , vol.176 , pp. 2822-2827
    • Salamitou, S.1    Raynaud, O.2    Lemaire, M.3    Coughton, M.4    Béguin, P.5    Aubert, J.P.6
  • 32
    • 0026569381 scopus 로고
    • Structure of the Clostridium thermocellum gene licB and the encoded β-1,3-1,4-glucanase
    • Schimming, S., Schwarz, W. H. & Staudenbauer, W. L. (1992). Structure of the Clostridium thermocellum gene licB and the encoded β-1,3-1,4-glucanase. Eur J Biochem 204, 13-19.
    • (1992) Eur J Biochem , vol.204 , pp. 13-19
    • Schimming, S.1    Schwarz, W.H.2    Staudenbauer, W.L.3
  • 33
    • 0026446384 scopus 로고
    • Rhamnogalacturonan acetylesterase: A novel enzyme from Aspergillus aculeatus, specific for the deacetylation of hairy (ramified) regimes of pectins
    • Searle-van Leeuwen, H. J. F., van den Brock, H., Schols, H. A., Beldman, G. & Voragen, A. G. J. (1992). Rhamnogalacturonan acetylesterase: a novel enzyme from Aspergillus aculeatus, specific for the deacetylation of hairy (ramified) regimes of pectins. Appl Microbiol Biotechnol 38, 347-349.
    • (1992) Appl Microbiol Biotechnol , vol.38 , pp. 347-349
    • Searle-Van Leeuwen, H.J.F.1    Van Den Brock, H.2    Schols, H.A.3    Beldman, G.4    Voragen, A.G.J.5
  • 34
    • 0028834125 scopus 로고
    • Analysis of DNA flanking the xynB locus of Streptomyces lividans reveals genes encoding acetyl xylan esterase and the RNA component of RnaseP
    • Shareck, F., Biely, P., Morosoli, R & Kluepfel, D. (1995). Analysis of DNA flanking the xynB locus of Streptomyces lividans reveals genes encoding acetyl xylan esterase and the RNA component of RnaseP. Gene 153, 105-109.
    • (1995) Gene , vol.153 , pp. 105-109
    • Shareck, F.1    Biely, P.2    Morosoli, R.3    Kluepfel, D.4
  • 35
    • 0030788755 scopus 로고    scopus 로고
    • Identification of a bacterial pectin acetylesterase in Erwinia chrysanthemi 3937
    • Shevchik, V. E. & Hugouvieux-Cotte-Pattat, N. (1997). Identification of a bacterial pectin acetylesterase in Erwinia chrysanthemi 3937. Mol Microbiol 24, 1285-1301.
    • (1997) Mol Microbiol , vol.24 , pp. 1285-1301
    • Shevchik, V.E.1    Hugouvieux-Cotte-Pattat, N.2
  • 36
    • 0029007122 scopus 로고
    • A new family of lipolytic enzymes?
    • Upton, C. & Buckley, J. T. (1995). A new family of lipolytic enzymes? Trends Biochem Sci 20, 178-179.
    • (1995) Trends Biochem Sci , vol.20 , pp. 178-179
    • Upton, C.1    Buckley, J.T.2
  • 37
    • 0031662992 scopus 로고    scopus 로고
    • Hairy plant polysaccharides: A close shave with microbial esterases
    • Williamson, G., Kroon, P. A. & Faulds, C. R. (1998). Hairy plant polysaccharides: a close shave with microbial esterases. Microbiology 144, 2011-2023.
    • (1998) Microbiology , vol.144 , pp. 2011-2023
    • Williamson, G.1    Kroon, P.A.2    Faulds, C.R.3
  • 38
    • 38249040868 scopus 로고
    • The effect of acetyl groups on the hydrolysis of ryegrass cell walls by xylanase and cellulase from Trichoderma koningii
    • Wood, T. M. & McCrae, S. I. (1986). The effect of acetyl groups on the hydrolysis of ryegrass cell walls by xylanase and cellulase from Trichoderma koningii. Phytochemistry 25, 1053-1055.
    • (1986) Phytochemistry , vol.25 , pp. 1053-1055
    • Wood, T.M.1    McCrae, S.I.2
  • 40
    • 0027945130 scopus 로고
    • Identification of non-catalytic conserved regions in xylanases encoded by the xynB and xynD genes of the cellulolytic rumen anaerobe Ruminococcus flavefaciens
    • Zhang, J.-X., Martin, J. & Flint, H. J. (1994). Identification of non-catalytic conserved regions in xylanases encoded by the xynB and xynD genes of the cellulolytic rumen anaerobe Ruminococcus flavefaciens. Mol Gen Genet 245, 260-264.
    • (1994) Mol Gen Genet , vol.245 , pp. 260-264
    • Zhang, J.-X.1    Martin, J.2    Flint, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.