메뉴 건너뛰기




Volumn 181, Issue 10, 1999, Pages 3284-3287

The type II pullulanase of Thermococcus hydrothermalis: Molecular characterization of the gene and expression of the catalytic domain

Author keywords

[No Author keywords available]

Indexed keywords

PULLULANASE; SIGNAL PEPTIDE;

EID: 0032908691     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.10.3284-3287.1999     Document Type: Article
Times cited : (79)

References (39)
  • 1
    • 0025300853 scopus 로고
    • Physiology and enzymology of thermophilic anaerobic bacteria degrading starch
    • Antranikian, G. 1990. Physiology and enzymology of thermophilic anaerobic bacteria degrading starch. FEMS Microbiol. Rev. 75:201-218.
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 201-218
    • Antranikian, G.1
  • 2
    • 0002331513 scopus 로고
    • Untersuchungen an pullulan
    • Bender, H., and K. Wallenfels. 1961. Untersuchungen an Pullulan. Biochem. Z. 334:79-95.
    • (1961) Biochem. Z. , vol.334 , pp. 79-95
    • Bender, H.1    Wallenfels, K.2
  • 3
    • 0027179678 scopus 로고
    • Characterization of amylolytic enzymes, having both α-1,4 and α-1,6 activity, from the thermophilic archaea Pyrococcus furiosus and Thermococcus litoralis
    • Brown, S. H., and R. M. Kelly. 1993. Characterization of amylolytic enzymes, having both α-1,4 and α-1,6 activity, from the thermophilic archaea Pyrococcus furiosus and Thermococcus litoralis. Appl. Environ. Microbiol. 59:2614-2621.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2614-2621
    • Brown, S.H.1    Kelly, R.M.2
  • 4
    • 0028171099 scopus 로고
    • Characterization of amylolytic and pullulytic enzymes from thermophilic archaea and from a new Fervidobacterium species
    • Canganella, F., C. M. Antrade, and G. Antranikian. 1994. Characterization of amylolytic and pullulytic enzymes from thermophilic archaea and from a new Fervidobacterium species. Appl. Microbiol. Biotechnol. 42:239-245.
    • (1994) Appl. Microbiol. Biotechnol. , vol.42 , pp. 239-245
    • Canganella, F.1    Antrade, C.M.2    Antranikian, G.3
  • 5
    • 0031014881 scopus 로고    scopus 로고
    • The S-layer protein of Corynebacterium glutamicum is anchored to the cell wall by its C-terminal hydrophobic domain
    • Chami, M., N. Bayan, J.-L. Peyret, T. Gulik-Krzywicki, G. Leblon, and E. Schechter. 1997. The S-layer protein of Corynebacterium glutamicum is anchored to the cell wall by its C-terminal hydrophobic domain. Mol. Microbiol. 23:483-492.
    • (1997) Mol. Microbiol. , vol.23 , pp. 483-492
    • Chami, M.1    Bayan, N.2    Peyret, J.-L.3    Gulik-Krzywicki, T.4    Leblon, G.5    Schechter, E.6
  • 6
    • 0344386178 scopus 로고    scopus 로고
    • S-layer and ABC transporter genes in methanogenic archaea
    • Conway de Macario, E., and A. J. L. Macario. 1997. S-layer and ABC transporter genes in methanogenic archaea. FEMS Microbiol. Rev. 20:59-64.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 59-64
    • Conway De Macario, E.A.1    Macario, A.J.L.2
  • 7
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. 1988. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:10881-10890.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 8
    • 0024712936 scopus 로고
    • Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: A potential new regulatory site in the interoperonic region
    • Dahl, M. K., E. Francoz, W. Saurin, W. Boos, M. D. Manson, and M. Hofnung. 1989. Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the interoperonic region. Mol. Gen. Genet. 218:199-207.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 199-207
    • Dahl, M.K.1    Francoz, E.2    Saurin, W.3    Boos, W.4    Manson, M.D.5    Hofnung, M.6
  • 9
    • 0022125681 scopus 로고
    • Sequence of gene malG in E. coli K12: Homologies between integral membrane components from binding protein-dependent transport systems
    • Dassa, E., and M. Hofnung. 1985. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 4:2287-2293.
    • (1985) EMBO J. , vol.4 , pp. 2287-2293
    • Dassa, E.1    Hofnung, M.2
  • 10
    • 0030803307 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
    • Dong, G., C. Vieille, and J. G. Zeikus. 1997. Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl. Environ. Microbiol. 63:3577-3584.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3577-3584
    • Dong, G.1    Vieille, C.2    Zeikus, J.G.3
  • 11
    • 0031991241 scopus 로고    scopus 로고
    • Purification and properties of an amylopullulanase, a glucoamylase and an α-glucosidase in the amylolytic enzyme system of Thermoanaerobacterium thermosaccharolyticum
    • Ganghofner, D., J. Kellermann, W. L. Staudenbauer, and K. Bronnenmeier. 1998. Purification and properties of an amylopullulanase, a glucoamylase and an α-glucosidase in the amylolytic enzyme system of Thermoanaerobacterium thermosaccharolyticum. Biosci. Biotechnol. Biochem. 62:302-308.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 302-308
    • Ganghofner, D.1    Kellermann, J.2    Staudenbauer, W.L.3    Bronnenmeier, K.4
  • 12
    • 0031809735 scopus 로고    scopus 로고
    • Purification and properties of a thermoactive and thermostable pullulanase from Thermococcus hydrothermalis, a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
    • Gantelet, H., and P. Duchiron. 1998. Purification and properties of a thermoactive and thermostable pullulanase from Thermococcus hydrothermalis, a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent. Appl. Microbiol. Biotechnol. 49:770-777.
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 770-777
    • Gantelet, H.1    Duchiron, P.2
  • 13
    • 0031667894 scopus 로고    scopus 로고
    • Characteristics of pullulanases from extremely thermophilic archaea isolated from deep-sea hydrothermal vents
    • Gantelet, H., C. Ladrat, A. Godfroy, G. Barbier, and F. Duchiron. 1998. Characteristics of pullulanases from extremely thermophilic archaea isolated from deep-sea hydrothermal vents. Biotechnol. Lett. 20:819-823.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 819-823
    • Gantelet, H.1    Ladrat, C.2    Godfroy, A.3    Barbier, G.4    Duchiron, F.5
  • 14
    • 0020491365 scopus 로고
    • Sequence of the malk gene in E. coli K12
    • Gilson, E., H. Nikaido, and M. Hofnung. 1982. Sequence of the malK gene in E. coli K12. Nucleic Acids Res. 25:7449-7458.
    • (1982) Nucleic Acids Res. , vol.25 , pp. 7449-7458
    • Gilson, E.1    Nikaido, H.2    Hofnung, M.3
  • 15
    • 0031888811 scopus 로고    scopus 로고
    • Archaeal binding protein-dependent ABC transporter: Molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis
    • Horlacher, R., K. B. Xavier, H. Santos, J. DiRuggiero, M. Kossman, and W. Boos. 1998. Archaeal binding protein-dependent ABC transporter: molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 180:680-689.
    • (1998) J. Bacteriol. , vol.180 , pp. 680-689
    • Horlacher, R.1    Xavier, K.B.2    Santos, H.3    Diruggiero, J.4    Kossman, M.5    Boos, W.6
  • 16
    • 0031913544 scopus 로고    scopus 로고
    • Cloning and expression of a Clostridium thermocellum xylanase gene in Escherichia coli
    • Jung, K. H., K. M. Lee, H. Kim, K. H. Yoon, S. H. Park, and M. Y. Pack. 1998. Cloning and expression of a Clostridium thermocellum xylanase gene in Escherichia coli. Biochem. Mol. Biol. Int. 44:283-292.
    • (1998) Biochem. Mol. Biol. Int. , vol.44 , pp. 283-292
    • Jung, K.H.1    Lee, K.M.2    Kim, H.3    Yoon, K.H.4    Park, S.H.5    Pack, M.Y.6
  • 17
    • 0023655597 scopus 로고
    • The primary structure of a prokaryotic glycoprotein
    • Lechner, J., and M. Sumper. 1987. The primary structure of a prokaryotic glycoprotein. J. Biol. Chem. 262:9724-9729.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9724-9729
    • Lechner, J.1    Sumper, M.2
  • 18
    • 0028146782 scopus 로고
    • Cloning of the aapT gene and characterization of its product, an amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601
    • Lee, S.-P., M. Morikawa, M. Takagi, and T. Imanaka. 1994. Cloning of the aapT gene and characterization of its product, an amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601. Appl. Environ. Microbiol. 60:3764-3773.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3764-3773
    • Lee, S.-P.1    Morikawa, M.2    Takagi, M.3    Imanaka, T.4
  • 19
    • 0031917122 scopus 로고    scopus 로고
    • Production of thermostable amylolytic enzymes by Thermococcus hydrothermalis
    • Legin, E., A. Copinet, and F. Duchiron. 1998. Production of thermostable amylolytic enzymes by Thermococcus hydrothermalis. Biotechnol. Lett. 20: 363-367.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 363-367
    • Legin, E.1    Copinet, A.2    Duchiron, F.3
  • 21
    • 0031983981 scopus 로고    scopus 로고
    • Identification of a region responsible for binding to the cell wall within the S-layer protein of Clostridium thermocellum
    • Lemaire, M., I. Miras, P. Gounon, and P. Béguin. 1998. Identification of a region responsible for binding to the cell wall within the S-layer protein of Clostridium thermocellum. Microbiology 144:211-217.
    • (1998) Microbiology , vol.144 , pp. 211-217
    • Lemaire, M.1    Miras, I.2    Gounon, P.3    Béguin, P.4
  • 22
    • 0029000658 scopus 로고
    • OlpB, a new outer layer protein of Clostridium thermocellum, and binding of its S-layer-like domain to components of the cell envelope
    • Lemaire, M., H. Ohayon, P. Gounon, T. Fujino, and P. Béguin. 1995. OlpB, a new outer layer protein of Clostridium thermocellum, and binding of its S-layer-like domain to components of the cell envelope. J. Bacteriol. 177: 2451-2459.
    • (1995) J. Bacteriol. , vol.177 , pp. 2451-2459
    • Lemaire, M.1    Ohayon, H.2    Gounon, P.3    Fujino, T.4    Béguin, P.5
  • 23
    • 0029769634 scopus 로고    scopus 로고
    • Purification and properties of a 140 kDa amylopullulanase from the thermophilic and alkaliphilic Bacillus sp. strain TS-23
    • Lin, L.-L., M.-R. Tsau, and W.-S. Chu. 1996. Purification and properties of a 140 kDa amylopullulanase from the thermophilic and alkaliphilic Bacillus sp. strain TS-23. Biotechnol. Appl. Biochem. 24:101-107.
    • (1996) Biotechnol. Appl. Biochem. , vol.24 , pp. 101-107
    • Lin, L.-L.1    Tsau, M.-R.2    Chu, W.-S.3
  • 24
    • 0028262129 scopus 로고
    • Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis
    • Lupas, A., H. Engelhardt, J. Peters, U. Santarius, S. Volker, and W. Baumeister. 1994. Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis. J. Bacteriol. 176:1224-1233.
    • (1994) J. Bacteriol. , vol.176 , pp. 1224-1233
    • Lupas, A.1    Engelhardt, H.2    Peters, J.3    Santarius, U.4    Volker, S.5    Baumeister, W.6
  • 25
    • 0027217955 scopus 로고
    • Improved purification and biochemical characterization of extracellular amylopullulanase from Thermoanaerobacter ethanolicus 39E
    • Mathupala, S. P., and J. G. Zeikus. 1993. Improved purification and biochemical characterization of extracellular amylopullulanase from Thermoanaerobacter ethanolicus 39E. Appl. Microbiol. Biotechnol. 39:487-493.
    • (1993) Appl. Microbiol. Biotechnol. , vol.39 , pp. 487-493
    • Mathupala, S.P.1    Zeikus, J.G.2
  • 26
    • 0028321448 scopus 로고
    • Pullulanase of Thermoanaerobacterium thermosulfurigenes EM 1 (Clostridium thermosulfurigenes): Molecular analysis of the enzyme and a common model for its attachment to the cell surface
    • Matuschek, M., G. Burchhardt, K. Sahm, and H. Bahl. 1994. Pullulanase of Thermoanaerobacterium thermosulfurigenes EM 1 (Clostridium thermosulfurigenes): molecular analysis of the enzyme and a common model for its attachment to the cell surface. J. Bacteriol. 176:3295-3302.
    • (1994) J. Bacteriol. , vol.176 , pp. 3295-3302
    • Matuschek, M.1    Burchhardt, G.2    Sahm, K.3    Bahl, H.4
  • 27
    • 0029853345 scopus 로고    scopus 로고
    • Characterization of genes from Thermoanaerobacterium thermomlfurigenes EM1 that encode two glycosyl hydrolases with conserved S-layer-like domains
    • Matuschek, M., K. Sahm, A. Zibat, and H. Bahl. 1996. Characterization of genes from Thermoanaerobacterium thermomlfurigenes EM1 that encode two glycosyl hydrolases with conserved S-layer-like domains. Mol. Gen. Genet. 252:493-496.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 493-496
    • Matuschek, M.1    Sahm, K.2    Zibat, A.3    Bahl, H.4
  • 28
    • 0028823497 scopus 로고
    • Conservation and variability in Archaea: Protein antigens with tandem repeats encoded by a cluster of genes with common motifs in Methanosarcina mazei S-6
    • Mayerhofer, L. E., E. Conway de Macario, and A. J. Macario. 1995. Conservation and variability in Archaea: protein antigens with tandem repeats encoded by a cluster of genes with common motifs in Methanosarcina mazei S-6. Gene 165:87-91.
    • (1995) Gene , vol.165 , pp. 87-91
    • Mayerhofer, L.E.1    Conway De Macario, E.2    Macario, A.J.3
  • 29
    • 7144262389 scopus 로고    scopus 로고
    • Structure, organization and expression of genes encoding for envelope components in the archaeon Methanosarcina mazei S-6
    • Mayerhofer, L. E., E. Conway de Macario, R. Yao, and A. J. Macario. 1998. Structure, organization and expression of genes encoding for envelope components in the archaeon Methanosarcina mazei S-6. Arch. Microbiol. 169: 339-345.
    • (1998) Arch. Microbiol. , vol.169 , pp. 339-345
    • Mayerhofer, L.E.1    Conway De Macario, E.2    Yao, R.3    Macario, A.J.4
  • 30
    • 0030825124 scopus 로고    scopus 로고
    • Glycoproteins in prokaryotes
    • Moens, S., and J. Vanderleyden. 1997. Glycoproteins in prokaryotes. Arch. Microbiol. 168:169-175.
    • (1997) Arch. Microbiol. , vol.168 , pp. 169-175
    • Moens, S.1    Vanderleyden, J.2
  • 31
    • 10144222885 scopus 로고    scopus 로고
    • A conserved motif in S-layer proteins is involved in peptidoglycan binding in Thermus thermophilus
    • Olabarria, G., J. L. Carrascosa, M. de Pedro, and J. Berenguer. 1996. A conserved motif in S-layer proteins is involved in peptidoglycan binding in Thermus thermophilus. J. Bacteriol. 178:4765-4772.
    • (1996) J. Bacteriol. , vol.178 , pp. 4765-4772
    • Olabarria, G.1    Carrascosa, J.L.2    De Pedro, M.3    Berenguer, J.4
  • 32
    • 0028144157 scopus 로고
    • Streptomyces lividans glycosylates the linker region of a β-1,4-glycanase from Cellulomonas fimi
    • Ong, E., D. G. Kilburn, R. C. Miller, and R. A. J. Warren. 1994. Streptomyces lividans glycosylates the linker region of a β-1,4-glycanase from Cellulomonas fimi. J. Bacteriol. 176:999-1008.
    • (1994) J. Bacteriol. , vol.176 , pp. 999-1008
    • Ong, E.1    Kilburn, D.G.2    Miller, R.C.3    Warren, R.A.J.4
  • 33
    • 0020638192 scopus 로고
    • A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides
    • Periman, D., and H. O. Halvorson. 1983. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J. Mol. Biol. 167:391-409.
    • (1983) J. Mol. Biol. , vol.167 , pp. 391-409
    • Periman, D.1    Halvorson, H.O.2
  • 34
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley, A. 1993. The complete general secretory pathway in Gram-negative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.1
  • 35
    • 0028859745 scopus 로고
    • Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli
    • Rüdiger, A., P. L. Jorgensen, and G. Antrinikian. 1995. Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli. Appl. Environ. Microbiol. 61:567-575.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 567-575
    • Rüdiger, A.1    Jorgensen, P.L.2    Antrinikian, G.3
  • 36
    • 0032415871 scopus 로고    scopus 로고
    • Identification of two binding domains, one for peptidoglycan and another for a secondary cell wall polymer, on the N-terminal part of the S-layer protein SbsB from Bacillus stearothermophilus PV72/p2
    • Sàra, M., E. M. Egelseer, C. Dekitsch, and U. B. Sleytr. 1998. Identification of two binding domains, one for peptidoglycan and another for a secondary cell wall polymer, on the N-terminal part of the S-layer protein SbsB from Bacillus stearothermophilus PV72/p2. J. Bacteriol. 180:6780-6783.
    • (1998) J. Bacteriol. , vol.180 , pp. 6780-6783
    • Sàra, M.1    Egelseer, E.M.2    Dekitsch, C.3    Sleytr, U.B.4
  • 37
    • 0029125175 scopus 로고
    • Functional analysis of the threonine- and serine-rich Gp-1 domain of glucoamylase I from Aspergillus awamori var. Kawachi
    • Semimaru, T., M. Goto, K. Furukawa, and S. Hayashida. 1995. Functional analysis of the threonine- and serine-rich Gp-1 domain of glucoamylase I from Aspergillus awamori var. Kawachi. Appl. Environ. Microbiol. 61:2885-2890.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2885-2890
    • Semimaru, T.1    Goto, M.2    Furukawa, K.3    Hayashida, S.4
  • 38
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. i
    • Sumper, M., E. Berg, R. Mengele, and I. Strobel. 1990. Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. i. Bacteriol. 172: 7111-7118.
    • (1990) Bacteriol. , vol.172 , pp. 7111-7118
    • Sumper, M.1    Berg, E.2    Mengele, R.3    Strobel, I.4
  • 39
    • 0026028264 scopus 로고
    • A hyperthermostable pullulanase produced by an extreme thermophile, Bacillus flavocaldarius KP 1228, and evidence for the proline theory of increasing protein thermostability
    • Suzuki, Y., K. Hatagaki, and H. Oda. 1991. A hyperthermostable pullulanase produced by an extreme thermophile, Bacillus flavocaldarius KP 1228, and evidence for the proline theory of increasing protein thermostability. Appl. Microbiol. Biotechnol. 34:707-714.
    • (1991) Appl. Microbiol. Biotechnol. , vol.34 , pp. 707-714
    • Suzuki, Y.1    Hatagaki, K.2    Oda, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.