메뉴 건너뛰기




Volumn 182, Issue 5, 2000, Pages 1346-1351

Feruloyl esterase activity of the Clostridium thermocellum cellulosome can be attributed to previously unknown domains of XynY and XynZ

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE DERIVATIVE; ESTERASE; FERULIC ACID; FERULOYL ESTERASE; ISOENZYME; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE; XYLOSE;

EID: 0033983751     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.5.1346-1351.2000     Document Type: Article
Times cited : (130)

References (44)
  • 3
    • 0030889272 scopus 로고    scopus 로고
    • Biochemical and antigenic characterization of a new dipeptidyl-peptidase isolated from Aspergillus fumigatus
    • Beauvais, A., M. Monod, J. P. Debeaupui, M. Diaquin, H. Kobayashi, and J. P. Latge. 1997. Biochemical and antigenic characterization of a new dipeptidyl-peptidase isolated from Aspergillus fumigatus. J. Biol. Chem. 272: 6238-6244.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6238-6244
    • Beauvais, A.1    Monod, M.2    Debeaupui, J.P.3    Diaquin, M.4    Kobayashi, H.5    Latge, J.P.6
  • 4
    • 0030002212 scopus 로고    scopus 로고
    • The cellulosome: An exocellular, multiprotein complex specialized in cellulose degradation
    • Béguin, P., and M. Lemaire. 1996. The cellulosome: an exocellular, multiprotein complex specialized in cellulose degradation. Crit. Rev. Biochem. Mol. Biol. 31:201-236.
    • (1996) Crit. Rev. Biochem. Mol. Biol. , vol.31 , pp. 201-236
    • Béguin, P.1    Lemaire, M.2
  • 5
    • 0041295729 scopus 로고    scopus 로고
    • Phenolic acid esterase activity of Clostridium thermocellum cellulosome is attributed to previously unknown domains of XynY and XynZ
    • K. Ohmiya, K. Hayashi, K. Sakka, Y. Kobayashi, S. Karita, and T. Kimura (ed.), Genetics, Biochemistry, and Ecology of Cellulose Degradation. UNI Publishers Co., Tokyo, Japan
    • Blum, D. L., I. Kataeva, X.-L. Li, and L. G. Ljungdahl. 1998. Phenolic acid esterase activity of Clostridium thermocellum cellulosome is attributed to previously unknown domains of XynY and XynZ, p. 478. In K. Ohmiya, K. Hayashi, K. Sakka, Y. Kobayashi, S. Karita, and T. Kimura (ed.), Genetics, Biochemistry, and Ecology of Cellulose Degradation. Proceedings of Mie Bioforum 98. UNI Publishers Co., Tokyo, Japan.
    • (1998) Proceedings of Mie Bioforum 98 , pp. 478
    • Blum, D.L.1    Kataeva, I.2    Li, X.-L.3    Ljungdahl, L.G.4
  • 6
    • 0032824378 scopus 로고    scopus 로고
    • Characterization of an acetyl xylan esterase from the anaerobic fungus Orpinomyces sp. strain PC-2
    • Blum, D. L., X.-L. Li, H. Chen, and L. G. Ljungdahl. 1999. Characterization of an acetyl xylan esterase from the anaerobic fungus Orpinomyces sp. strain PC-2. Appl. Environ. Microbiol. 65:3990-3995.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3990-3995
    • Blum, D.L.1    Li, X.-L.2    Chen, H.3    Ljungdahl, L.G.4
  • 7
    • 0025012288 scopus 로고
    • Assay for trans-p-coumaroyl esterase using a specific substrate from plant cell walls
    • Borneman, W. S., R. D. Hartley, D. S. Himmelsbach, and L. G. Ljungdahl. 1990. Assay for trans-p-coumaroyl esterase using a specific substrate from plant cell walls. Anal. Biochem. 190:129-133.
    • (1990) Anal. Biochem. , vol.190 , pp. 129-133
    • Borneman, W.S.1    Hartley, R.D.2    Himmelsbach, D.S.3    Ljungdahl, L.G.4
  • 8
    • 0002025596 scopus 로고
    • Feruloyl and p-coumaroyl esterases from the anaerobic fungus Neocallimastix MC-2: Properties and functions in plant cell wall degradation
    • M. P. Coughlan and G. Hazlewood (ed.), Portland Press, Cambridge, United Kingdom
    • Borneman, W. S., L. G. Ljungdahl, R. D. Hartley, and D. E. Akin. 1993. Feruloyl and p-coumaroyl esterases from the anaerobic fungus Neocallimastix MC-2: properties and functions in plant cell wall degradation, p. 85-102. In M. P. Coughlan and G. Hazlewood (ed.), Hemicellulose and hemicellulases. Portland Press, Cambridge, United Kingdom.
    • (1993) Hemicellulose and Hemicellulases , pp. 85-102
    • Borneman, W.S.1    Ljungdahl, L.G.2    Hartley, R.D.3    Akin, D.E.4
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0027210404 scopus 로고
    • DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: Organizational symmetry around the origin of replication
    • Burland, V. D., G. Plunkett III, D. L. Daniels, and F. R. Blattner. 1993. DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics 16:551-561.
    • (1993) Genomics , vol.16 , pp. 551-561
    • Burland, V.D.1    Plunkett G. III2    Daniels, D.L.3    Blattner, F.R.4
  • 11
    • 0001523970 scopus 로고    scopus 로고
    • Dissociation of the cellulosome of Clostridium thermocellum in the presence of ethylenediaminetetraacetic acid occurs with the formation of truncated polypeptides
    • Choi, S. K., and L. G. Ljungdahl. 1996. Dissociation of the cellulosome of Clostridium thermocellum in the presence of ethylenediaminetetraacetic acid occurs with the formation of truncated polypeptides. Biochemistry 35:4897-4905.
    • (1996) Biochemistry , vol.35 , pp. 4897-4905
    • Choi, S.K.1    Ljungdahl, L.G.2
  • 13
    • 0030927036 scopus 로고    scopus 로고
    • Expression of a Butyrivibrio fibrisolvens E14 gene (cinB) encoding an enzyme with cinnamoyl esterase activity is negatively regulated by the product of an adjacent gene (cinR)
    • Dalrymple, B. D., and Y. Swadling. 1997. Expression of a Butyrivibrio fibrisolvens E14 gene (cinB) encoding an enzyme with cinnamoyl esterase activity is negatively regulated by the product of an adjacent gene (cinR). Microbiology 143:1203-1210.
    • (1997) Microbiology , vol.143 , pp. 1203-1210
    • Dalrymple, B.D.1    Swadling, Y.2
  • 14
    • 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. D., Y. Swadling, D. H. Cybinski, and G.-P. Xue. 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.D.1    Swadling, Y.2    Cybinski, D.H.3    Xue, G.-P.4
  • 17
    • 0028786027 scopus 로고
    • The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic rumen fungi functions as a docking domain
    • Fanutti, C., T. Ponyi, G. W. Black, G. P. Hazlewood, and H. J. Gilbert. 1995. The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic rumen fungi functions as a docking domain. J. Biol. Chem. 270:29314-29322.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29314-29322
    • Fanutti, C.1    Ponyi, T.2    Black, G.W.3    Hazlewood, G.P.4    Gilbert, H.J.5
  • 18
    • 0027169343 scopus 로고
    • A modular esterase from Pseudomonas fluorescens subsp. cellulosa contains a non-catalytic cellulose-binding domain
    • Ferreira, L. M. A., T. M. Wood, G. Williamson, C. Faulds, G. P. Hazlewood, G. W. Black, and H. J. Gilbert, 1993. A modular esterase from Pseudomonas fluorescens subsp. cellulosa contains a non-catalytic cellulose-binding domain. Biochem. J. 294:349-355.
    • (1993) Biochem. J. , vol.294 , pp. 349-355
    • Ferreira, L.M.A.1    Wood, T.M.2    Williamson, G.3    Faulds, C.4    Hazlewood, G.P.5    Black, G.W.6    Gilbert, H.J.7
  • 19
    • 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., J. Martin, C. A. McPherson, A. S. Daniel, and J.-X. Zhang. 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, C.A.3    Daniel, A.S.4    Zhang, J.-X.5
  • 20
    • 0028949132 scopus 로고
    • Evidence for a general role for noncatalytic thermostabilizing domains in xylananses from thermophilic bacteria
    • Fontes, C. M. G. A., G. P. Hazlewood, E. Morag, J. Hall, B. H. Hirst, and H. J. Gilbert. 1995. Evidence for a general role for noncatalytic thermostabilizing domains in xylananses from thermophilic bacteria. Biochem. J. 307: 151-158.
    • (1995) Biochem. J. , vol.307 , pp. 151-158
    • Fontes, C.M.G.A.1    Hazlewood, G.P.2    Morag, E.3    Hall, J.4    Hirst, B.H.5    Gilbert, H.J.6
  • 21
    • 0026640499 scopus 로고
    • Homologous catalytic domains in a rumen fungal xylanase: Evidence for gene duplication and prokaryotic origin
    • Gilbert, H. J., G. P. Hazlewood, J. I. Laurie, C. G. Orpin, and G. P. Xue. 1992. Homologous catalytic domains in a rumen fungal xylanase: evidence for gene duplication and prokaryotic origin. Mol. Microbiol. 6:2065-2072.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2065-2072
    • Gilbert, H.J.1    Hazlewood, G.P.2    Laurie, J.I.3    Orpin, C.G.4    Xue, G.P.5
  • 22
    • 0024094694 scopus 로고
    • Purification of Clostridium thermocellum xylanase Z expressed in Escherichia coli and identification of the corresponding product in the culture medium of C. thermocellum
    • Grépinet, O., M.-C. Chebrou, and P. Béguin. 1988. Purification of Clostridium thermocellum xylanase Z expressed in Escherichia coli and identification of the corresponding product in the culture medium of C. thermocellum. J. Bacteriol. 170:4576-4581.
    • (1988) J. Bacteriol. , vol.170 , pp. 4576-4581
    • Grépinet, O.1    Chebrou, M.-C.2    Béguin, P.3
  • 23
    • 0032937839 scopus 로고    scopus 로고
    • Nucleotide sequences of two contiguous and highly homologous xylanase genes xynA and xynB and characterization of xynA from Clostridium thermocellum
    • Hayashi, H., M. Takehara, T. Hattori, T. Kimura, S. Karita, K. Sakka, and K. Ohmiya. 1999. Nucleotide sequences of two contiguous and highly homologous xylanase genes xynA and xynB and characterization of XynA from Clostridium thermocellum. Appl. Microbiol. Biotechnol. 51:348-357.
    • (1999) Appl. Microbiol. Biotechnol. , vol.51 , pp. 348-357
    • Hayashi, H.1    Takehara, M.2    Hattori, T.3    Kimura, T.4    Karita, S.5    Sakka, K.6    Ohmiya, K.7
  • 24
    • 0032857727 scopus 로고    scopus 로고
    • Cloning and sequence analysis of a new cellulase gene encoding celK, a major cellulosome component of Clostridium thermocellum: Evidence for gene duplication and recombination
    • Kataeva, I., X.-L. Li, H. Chen, S.-K Choi, and L. G. Ljungdahl. 1999. Cloning and sequence analysis of a new cellulase gene encoding CelK, a major cellulosome component of Clostridium thermocellum: evidence for gene duplication and recombination. J. Bacteriol. 181:5288-5295.
    • (1999) J. Bacteriol. , vol.181 , pp. 5288-5295
    • Kataeva, I.1    Li, X.-L.2    Chen, H.3    Choi, S.-K.4    Ljungdahl, L.G.5
  • 25
    • 17744414050 scopus 로고    scopus 로고
    • Plant cell wall degrading enzyme complexes from the cellulolytic rumen bacterium Ruminococcus flavefaciens
    • Kirby, J., V. Aurilia, S. I. McCrae, J. C. Martin, and H. J. Flint. 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
  • 26
    • 0025690514 scopus 로고
    • Subunit composition and glycosidic activities of the cellulase complex from Clostridium thermocellum JW20
    • Kohring, S., J. Wiegel, and F. Mayer. 1990. Subunit composition and glycosidic activities of the cellulase complex from Clostridium thermocellum JW20. Appl. Environ. Microbiol. 56:3798-3804.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3798-3804
    • Kohring, S.1    Wiegel, J.2    Mayer, F.3
  • 27
    • 0030796446 scopus 로고    scopus 로고
    • Identification of a naturally occurring peroxidase-lipoxygenase fusion protein
    • Koljak, R., O. Boutaud, B.-H. Shieh, N. Samel, and A. R. Brash. 1997. Identification of a naturally occurring peroxidase-lipoxygenase fusion protein. Science 277:1994-1996.
    • (1997) Science , vol.277 , pp. 1994-1996
    • Koljak, R.1    Boutaud, O.2    Shieh, B.-H.3    Samel, N.4    Brash, A.R.5
  • 28
    • 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
  • 29
    • 0021016163 scopus 로고
    • Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum
    • Lamed, R., E. Setter, and E. A. Bayer. 1983. Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum. J. Bacteriol. 156:828-836.
    • (1983) J. Bacteriol. , vol.156 , pp. 828-836
    • Lamed, R.1    Setter, E.2    Bayer, E.A.3
  • 30
    • 0020958567 scopus 로고
    • The cellulosome - A discrete cell surface organelle of Clostridium thermocellum which exhibits separate antigenic, cellulose-binding and various cellulolytic activities
    • Lamed, R., E. Setter, R. Kenig, and E. A. Bayer. 1983. The cellulosome - a discrete cell surface organelle of Clostridium thermocellum which exhibits separate antigenic, cellulose-binding and various cellulolytic activities. Biotechnol. Bioeng. Symp. 13:163-181.
    • (1983) Biotechnol. Bioeng. Symp. , vol.13 , pp. 163-181
    • Lamed, R.1    Setter, E.2    Kenig, R.3    Bayer, E.A.4
  • 32
    • 0030780751 scopus 로고    scopus 로고
    • Two cellulases, CelA and CelC, from the polycentric anaerobic fungus Orpinomyces strain PC-2 contain N-terminal docking domains for a cellulase-hemicellulase complex
    • Li, X.-L., H. Chen, and L. G. Ljungdahl. 1997. Two cellulases, CelA and CelC, from the polycentric anaerobic fungus Orpinomyces strain PC-2 contain N-terminal docking domains for a cellulase-hemicellulase complex. Appl. Environ. Microbiol. 63:4721-4728.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4721-4728
    • Li, X.-L.1    Chen, H.2    Ljungdahl, L.G.3
  • 33
    • 0010445312 scopus 로고
    • Macrocellulase complexes and yellow affinity substance from Clostridium thermocellum
    • Ljungdahl, L. G., M. P. Coughlan, F. Mayer, Y. Mori, and K. Hon-nami. 1988. Macrocellulase complexes and yellow affinity substance from Clostridium thermocellum. Methods Enzymol. 160:483-500.
    • (1988) Methods Enzymol. , vol.160 , pp. 483-500
    • Ljungdahl, L.G.1    Coughlan, M.P.2    Mayer, F.3    Mori, Y.4    Hon-Nami, K.5
  • 34
    • 0018877176 scopus 로고
    • Methylene-tetrahydrofolate dehydrogenase from Clostridium formicoaceticum and methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase (combined) from Clostridium thermoaceticum
    • Ljungdahl, L. G., W. E. O'Brien, M. R. Moore, and M.-T. Liu. 1980. Methylene-tetrahydrofolate dehydrogenase from Clostridium formicoaceticum and methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase (combined) from Clostridium thermoaceticum. Methods Enzymol. 66:599-609.
    • (1980) Methods Enzymol. , vol.66 , pp. 599-609
    • Ljungdahl, L.G.1    O'Brien, W.E.2    Moore, M.R.3    Liu, M.-T.4
  • 35
    • 0031959756 scopus 로고    scopus 로고
    • Butyrivibrio spp. and other xylanolytic microorganisms from the rumen have cinnamoyl esterase activity
    • McSweeney, C. S., A. Dulieu, and R. Bunch. 1998. Butyrivibrio spp. and other xylanolytic microorganisms from the rumen have cinnamoyl esterase activity. Anaerobe 4:57-65.
    • (1998) Anaerobe , vol.4 , pp. 57-65
    • McSweeney, C.S.1    Dulieu, A.2    Bunch, R.3
  • 36
    • 0027989660 scopus 로고
    • Solubilization of lignin by the ruminal anaerobic fungus Neocallimastix patriciarum
    • McSweeney, C. S., A. Dulieu, Y. Katayama, and J. B. Lowry. 1994. Solubilization of lignin by the ruminal anaerobic fungus Neocallimastix patriciarum. Appl. Environ. Microbiol. 60:2985-2989.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2985-2989
    • McSweeney, C.S.1    Dulieu, A.2    Katayama, Y.3    Lowry, J.B.4
  • 37
    • 33747333106 scopus 로고
    • Use of dinitrosaliclic acid reagent for determination of reducing sugars
    • Miller, G. L. 1959. Use of dinitrosaliclic acid reagent for determination of reducing sugars. Anal. Chem. 31:127-132.
    • (1959) Anal. Chem. , vol.31 , pp. 127-132
    • Miller, G.L.1
  • 38
    • 0026848803 scopus 로고
    • Affinity digestion for the near-total recovery of purified cellulosome from Clostridium thermocellum
    • Morag, E., E. A. Bayer, and R. Lamed. 1992. Affinity digestion for the near-total recovery of purified cellulosome from Clostridium thermocellum. Enzyme Microb. Technol. 14:289-292.
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 289-292
    • Morag, E.1    Bayer, E.A.2    Lamed, R.3
  • 39
    • 0029117332 scopus 로고
    • Lignin-ferulate cross-links in grasses: Active incorporation of ferulate polysaccharides esters into ryegrass lignins
    • Ralph, J., J. H. Grabber, and R. D. Hatfield. 1995. Lignin-ferulate cross-links in grasses: active incorporation of ferulate polysaccharides esters into ryegrass lignins. Carbohydr. Res. 275:167-178.
    • (1995) Carbohydr. Res. , vol.275 , pp. 167-178
    • Ralph, J.1    Grabber, J.H.2    Hatfield, R.D.3
  • 40
    • 0030269964 scopus 로고    scopus 로고
    • The rumen: A unique source of enzymes for enhancing livestock production
    • Selinger, L. B., C. W. Forsberg, and K.-J. Cheng. 1996. The rumen: a unique source of enzymes for enhancing livestock production. Anaerobe 2:263-284.
    • (1996) Anaerobe , vol.2 , pp. 263-284
    • Selinger, L.B.1    Forsberg, C.W.2    Cheng, K.-J.3
  • 42
    • 0028316750 scopus 로고
    • Crystallization and preliminary diffraction analysis of the catalytic domain of xylanase Z from Clostridium thermocellum
    • Souchon, H., S. Spinelli, P. Béguin, and P. M. Alzari. 1994. Crystallization and preliminary diffraction analysis of the catalytic domain of xylanase Z from Clostridium thermocellum. J. Mol. Biol. 235:1348-1350.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1348-1350
    • Souchon, H.1    Spinelli, S.2    Béguin, P.3    Alzari, P.M.4
  • 43
    • 0038850044 scopus 로고
    • Multifunctional proteins: One gene - More than one enzyme
    • Stark, G. R. 1977. Multifunctional proteins: one gene - more than one enzyme. Trends Biochem. Sci. 2:64-66.
    • (1977) Trends Biochem. Sci. , vol.2 , pp. 64-66
    • Stark, G.R.1
  • 44
    • 0031662992 scopus 로고    scopus 로고
    • Hairy plant polysaccharides: A close shave with microbial esterases
    • Williamson, G., P. A. Kroon, and C. B. Faulds. 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.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.