메뉴 건너뛰기




Volumn 65, Issue 9, 1999, Pages 3990-3995

Characterization of an acetyl xylan esterase from the anaerobic fungus Orpinomyces sp. strain PC-2

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLXYLAN ESTERASE; AMINO ACID; COMPLEMENTARY DNA; ESTERASE; FUNGAL DNA; UNCLASSIFIED DRUG; XYLAN;

EID: 0032824378     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.65.9.3990-3995.1999     Document Type: Article
Times cited : (80)

References (32)
  • 1
    • 0025095637 scopus 로고
    • Supernatant protein and cellulase activities of the anaerobic ruminal fungus Neocallimastix frontalis EB188
    • Barichievich, E. M., and R. E. Calza. 1990. Supernatant protein and cellulase activities of the anaerobic ruminal fungus Neocallimastix frontalis EB188. Appl. Environ. Microbiol. 56:43-48.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 43-48
    • Barichievich, E.M.1    Calza, R.E.2
  • 2
    • 0024657936 scopus 로고
    • Fermentation products and plant cell wall-degrading enzymes produced by monocentric and polycentric anaerobic ruminai fungi
    • Borneman, W. S., D. E. Akin, and L. G. Ljungdahl. 1989. Fermentation products and plant cell wall-degrading enzymes produced by monocentric and polycentric anaerobic ruminai fungi. Appl. Environ. Microbiol. 55:1066-1073.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 1066-1073
    • Borneman, W.S.1    Akin, D.E.2    Ljungdahl, L.G.3
  • 3
    • 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
  • 4
    • 0002025596 scopus 로고
    • Feruloyl and p-coumaroyl esterases from the anaerobic fungus Neocallimastix strain MC-2: Properties and functions in plant cell wall degradation
    • M. P. Coughlan and G. P. Hazlewood (ed.), Portland Press, London, England
    • Borneman, W. S., L. G. Ljungdahl, R. D. Hartley, and D. E. Akin. 1993. Feruloyl and p-coumaroyl esterases from the anaerobic fungus Neocallimastix strain MC-2: properties and functions in plant cell wall degradation, p. 85-102. In M. P. Coughlan and G. P. Hazlewood (ed.), Hemicellulose and hemicellulases. Portland Press, London, England.
    • (1993) Hemicellulose and Hemicellulases , pp. 85-102
    • Borneman, W.S.1    Ljungdahl, L.G.2    Hartley, R.D.3    Akin, D.E.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0028920626 scopus 로고
    • A cyclophilin from the polycentric anaerobic rumen fungus Orpinomyces sp. strain PC-2 is highly homologous to vertebrate cyclophilin B
    • Chen, H., X. L. Li, and L. G. Ljungdahl. 1995. A cyclophilin from the polycentric anaerobic rumen fungus Orpinomyces sp. strain PC-2 is highly homologous to vertebrate cyclophilin B. Proc. Natl. Acad. Sci. USA 92:2587-2591.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2587-2591
    • Chen, H.1    Li, X.L.2    Ljungdahl, L.G.3
  • 7
    • 0030883632 scopus 로고    scopus 로고
    • Sequencing of a 1,3-1,4-beta-D-glucanase (lichenase) from the anaerobic fungus Orpinomyces strain PC-2: Properties of the enzyme expressed in Escherichia coli and evidence that the gene has a bacterial origin
    • Chen, H., X. L. Li, and L. G. Ljungdahl. 1997. Sequencing of a 1,3-1,4-beta-D-glucanase (lichenase) from the anaerobic fungus Orpinomyces strain PC-2: properties of the enzyme expressed in Escherichia coli and evidence that the gene has a bacterial origin. J. Bacteriol. 179:6028-6034.
    • (1997) J. Bacteriol. , vol.179 , pp. 6028-6034
    • Chen, H.1    Li, X.L.2    Ljungdahl, L.G.3
  • 8
    • 0002030661 scopus 로고
    • Polysaccharide degradation by rumen microorganisms
    • P. N. Hobson (ed.), Elsevier Applied Science, New York, N.Y.
    • Chesson, A., and C. W. Forsberg. 1988. Polysaccharide degradation by rumen microorganisms, p. 251-284. In P. N. Hobson (ed.), The rumen microbial ecosystem. Elsevier Applied Science, New York, N.Y.
    • (1988) The Rumen Microbial Ecosystem , pp. 251-284
    • Chesson, A.1    Forsberg, C.W.2
  • 9
    • 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., D. H. Cybinski, I. Layton, C. S. McSweeney, G. P. Xue, Y. J. Swadling, and J. B. Lowry. 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
  • 11
    • 0028786027 scopus 로고
    • The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein 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 fungi functions as a protein 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
  • 12
    • 0344765499 scopus 로고    scopus 로고
    • Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain
    • Ghosh, D., W. Duax, H. Jornvall, and J. Eyzaguirre. 1998. Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain. FEBS Lett. 423:35-38.
    • (1998) FEBS Lett. , vol.423 , pp. 35-38
    • Ghosh, D.1    Duax, W.2    Jornvall, H.3    Eyzaguirre, J.4
  • 13
    • 0028295908 scopus 로고
    • Purification and some characteristics of the acetyl xylan esterase from Schizophyllum commune
    • Halgasova, N., E. Kutejova, and J. Timko. 1994. Purification and some characteristics of the acetyl xylan esterase from Schizophyllum commune. Biochem. J. 298:751-755.
    • (1994) Biochem. J. , vol.298 , pp. 751-755
    • Halgasova, N.1    Kutejova, E.2    Timko, J.3
  • 14
    • 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 (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0026446384 scopus 로고
    • Rhamnogalacturonan acetylesterase: A novel enzyme from Aspergillus aculeatus, specific for the deacetylation of hairy (ramified) regions of pectins
    • Leeuwen, M. J. F. S.-v., L. A. M. v. d. Broek, J. A. Schols, G. Beldman, and A. G. J. Voragen. 1992. Rhamnogalacturonan acetylesterase: a novel enzyme from Aspergillus aculeatus, specific for the deacetylation of hairy (ramified) regions of pectins. Appl. Microbiol. Biotechnol. 38:347-349.
    • (1992) Appl. Microbiol. Biotechnol. , vol.38 , pp. 347-349
    • Leeuwen, M.J.F.S.-V.1    Broek, L.A.M.V.D.2    Schols, J.A.3    Beldman, G.4    Voragen, A.G.J.5
  • 16
    • 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
  • 17
    • 0030969313 scopus 로고    scopus 로고
    • Monocentric and polycentric anaerobic fungi produce structurally related cellulases and xylanases
    • Li, X.-L., H. Chen, and L. G. Ljungdahl. 1997. Monocentric and polycentric anaerobic fungi produce structurally related cellulases and xylanases. Appl. Environ. Microbiol. 63:628-635.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 628-635
    • Li, X.-L.1    Chen, H.2    Ljungdahl, L.G.3
  • 19
    • 0001740024 scopus 로고    scopus 로고
    • Evidence in anaerobic fungi of transfer of genes between them and from aerobic fungi, bacteria and animal hosts
    • J. Wiegel and M. W. W. Adams (ed.), Taylor and Francis, Inc., Philadelphia, Pa
    • Ljungdahl, L. G., X.-L. Li, and H. Z. Chen. 1998. Evidence in anaerobic fungi of transfer of genes between them and from aerobic fungi, bacteria and animal hosts, p. 187-197. In J. Wiegel and M. W. W. Adams (ed.), Thermophiles: the keys to molecular evolution and the origin of life? Taylor and Francis, Inc., Philadelphia, Pa.
    • (1998) Thermophiles: The Keys to Molecular Evolution and the Origin of Life , pp. 187-197
    • Ljungdahl, L.G.1    Li, X.-L.2    Chen, H.Z.3
  • 20
    • 0030886131 scopus 로고    scopus 로고
    • Isolation, analysis, and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: A β-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity
    • Lorenz, W. W., and J. Wiegel. 1997. Isolation, analysis, and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: a β-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity. J. Bacteriol. 179:5435-5441.
    • (1997) J. Bacteriol. , vol.179 , pp. 5435-5441
    • Lorenz, W.W.1    Wiegel, J.2
  • 21
    • 0025250489 scopus 로고
    • Overproduction of an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" in Escherichia coli
    • Luthi, E., N. B. Jasmat, and P. L. Bergquist. 1990. Overproduction of an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" in Escherichia coli. Appl. Microbiol. Biotechnol. 34:214-219.
    • (1990) Appl. Microbiol. Biotechnol. , vol.34 , pp. 214-219
    • Luthi, E.1    Jasmat, N.B.2    Bergquist, P.L.3
  • 22
    • 0029992163 scopus 로고    scopus 로고
    • Acetyl xylan esterase from Trichoderma reesei contains an active-site serine residue and a cellulose-binding domain
    • Margolles-Clark, E., M. Tenkanen, and M. Penttila. 1996. Acetyl xylan esterase from Trichoderma reesei contains an active-site serine residue and a cellulose-binding domain. Eur. J. Biochem. 237:553-560.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 553-560
    • Margolles-Clark, E.1    Tenkanen, M.2    Penttila, M.3
  • 23
    • 0025667926 scopus 로고
    • Purification and properties of an acetyl xylan esterase from Fibrobacter succinogenes
    • McDermid, K. P., C. W. Forsberg, and C. R. MacKenzie. 1990. Purification and properties of an acetyl xylan esterase from Fibrobacter succinogenes. Appl. Environ. Microbiol. 56:3805-3810.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3805-3810
    • McDermid, K.P.1    Forsberg, C.W.2    MacKenzie, C.R.3
  • 24
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu, H. C., and L. A. Heppel. 1965. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 240:3685-3692.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 26
    • 0016862399 scopus 로고
    • The quantitation of rat serum esterases by densitometry of acrylamide gels stained for enzyme activity
    • Rosenberg, M., V. Roegner, and F. F. Becker. 1975. The quantitation of rat serum esterases by densitometry of acrylamide gels stained for enzyme activity. Anal. Biochem. 66:206-212.
    • (1975) Anal. Biochem. , vol.66 , pp. 206-212
    • Rosenberg, M.1    Roegner, V.2    Becker, F.F.3
  • 27
    • 0030269964 scopus 로고    scopus 로고
    • The rumen: A unique source of enzymes for enhancing livestock production
    • Salinger, 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
    • Salinger, L.B.1    Forsberg, C.W.2    Cheng, K.-J.3
  • 28
    • 0028869651 scopus 로고
    • Purification and characterization of two thermostable acetyl xylan esterases from Thermoanerobacterium sp. strain JW/SL YS485
    • Shao, W., and J. Wiegel. 1995. Purification and characterization of two thermostable acetyl xylan esterases from Thermoanerobacterium sp. strain JW/SL YS485. Appl. Environ. Microbiol. 61:729-733.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 729-733
    • Shao, W.1    Wiegel, J.2
  • 29
    • 0028834125 scopus 로고
    • Analysis of DNA flanking the xlnB locus of Streptomyces lividans reveals genes encoding acetyl xylan esterase and the RNA component of ribonuclease P
    • Shareck, F., P. Biely, R. Morosoli, and D. Kluepfel. 1995. Analysis of DNA flanking the xlnB locus of Streptomyces lividans reveals genes encoding acetyl xylan esterase and the RNA component of ribonuclease P. Gene 153:105-109.
    • (1995) Gene , vol.153 , pp. 105-109
    • Shareck, F.1    Biely, P.2    Morosoli, R.3    Kluepfel, D.4
  • 30
    • 0030788755 scopus 로고    scopus 로고
    • Identification of a bacterial pectin acetyl esterase in Erwinia chrysanthemi 3937
    • Shevchik, V. E., and N. Hugouvieux-Cotte-Pattat. 1997. Identification of a bacterial pectin acetyl esterase 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
  • 31
    • 0040082893 scopus 로고    scopus 로고
    • Synergism among endo-xylanase, β-xylo-sidase, and acetyl xylan esterase from Bacillus steamthermophilus
    • Suh, J.-H., and C. Yong-Jin. 1996. Synergism among endo-xylanase, β-xylo-sidase, and acetyl xylan esterase from Bacillus steamthermophilus. J. Microbiol. Biotechnol. 6:173-178.
    • (1996) J. Microbiol. Biotechnol. , vol.6 , pp. 173-178
    • Suh, J.-H.1    Yong-Jin, C.2
  • 32
    • 0030892096 scopus 로고    scopus 로고
    • Cloning and sequence analysis of genes encoding xylanases and acetyl xylan esterase from Streptomyces thermaviolaceus OPC-520
    • Tsujibo, H., T. Ohtsuki, T. Iio, I. Yamazaki, K. Miyamoto, M. Sugiyama, and Y. Inamori. 1997. Cloning and sequence analysis of genes encoding xylanases and acetyl xylan esterase from Streptomyces thermaviolaceus OPC-520. Appl. Environ. Microbiol. 63:661-664.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 661-664
    • Tsujibo, H.1    Ohtsuki, T.2    Iio, T.3    Yamazaki, I.4    Miyamoto, K.5    Sugiyama, M.6    Inamori, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.