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Volumn 6, Issue 3, 2007, Pages 315-320

A unique thermostable lichenase from Thermotoga maritima MSB8 with divergent substrate specificity

Author keywords

Endoglucanase; Family 5; Glucosyl 1,3 glucosyl 1,4 glucose; Glucosyl 1,4 glucosyl 1,3 glucose; Lichenase; Thermotoga maritima

Indexed keywords

CELLULASE; GLUCAN SYNTHASE;

EID: 34548236457     PISSN: 09725849     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 0034047876 scopus 로고    scopus 로고
    • Mechanism of substrate hydrolysis by a thermophilic endoglucanase from Thermotoga maritima
    • Evans B R, Gilman A K, Cordray K & Woodward J, Mechanism of substrate hydrolysis by a thermophilic endoglucanase from Thermotoga maritima, Biotechnol Lett, 22 (2000) 735-740.
    • (2000) Biotechnol Lett , vol.22 , pp. 735-740
    • Evans, B.R.1    Gilman, A.K.2    Cordray, K.3    Woodward, J.4
  • 2
    • 0032403607 scopus 로고    scopus 로고
    • Purification, characterization, and molecular analysis of thermostable cellulases CelA and CelB from Thermotoga neapolitana
    • Bok J D, Yernool D A & Eveleigh D E, Purification, characterization, and molecular analysis of thermostable cellulases CelA and CelB from Thermotoga neapolitana, Appl Environ Microbiol, 64 (1998) 4774-4781.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4774-4781
    • Bok, J.D.1    Yernool, D.A.2    Eveleigh, D.E.3
  • 3
    • 0031437663 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of an endo- β-1,3-glucanase of the hyperthermophilic archaeon Pyrococcus furiosus
    • Gueguen Y, Voorhorst W G B, van der Oost J & de Vos W M, Molecular and biochemical characterization of an endo- β-1,3-glucanase of the hyperthermophilic archaeon Pyrococcus furiosus, J Biol Chem, 272 (1997) 31258-31264.
    • (1997) J Biol Chem , vol.272 , pp. 31258-31264
    • Gueguen, Y.1    Voorhorst, W.G.B.2    van der Oost, J.3    de Vos, W.M.4
  • 4
    • 0022522022 scopus 로고
    • Thermotoga maritima sp-nov represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C
    • Huber R, Langworthy T A, Konig H, Thomm M, Woese C R et al, Thermotoga maritima sp-nov represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C, Arch Microbiol, 144 (1986) 324-333.
    • (1986) Arch Microbiol , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.A.2    Konig, H.3    Thomm, M.4    Woese, C.R.5
  • 5
    • 0033609333 scopus 로고    scopus 로고
    • Evidence for lateral gene transfer between archaea and bacteria from genome sequence of Thermotoga maritima
    • Nelson K E, Clayton R A, Gill S R, Gwinn M L, Dodson R J et al, Evidence for lateral gene transfer between archaea and bacteria from genome sequence of Thermotoga maritima, Nature (Lond), 399 (1999) 323-329.
    • (1999) Nature (Lond , vol.399 , pp. 323-329
    • Nelson, K.E.1    Clayton, R.A.2    Gill, S.R.3    Gwinn, M.L.4    Dodson, R.J.5
  • 6
    • 34548286979 scopus 로고    scopus 로고
    • Characterization of an endo- β-1,4- glucanase of Thermotoga maritima expressed in Escherichia coli
    • Rahman M M, Bhuiyan S H, Nirasawa S, Kitaoka M & Hayashi K, Characterization of an endo- β-1,4- glucanase of Thermotoga maritima expressed in Escherichia coli, J Appl Glycosci, 49 (2002) 487-495.
    • (2002) J Appl Glycosci , vol.49 , pp. 487-495
    • Rahman, M.M.1    Bhuiyan, S.H.2    Nirasawa, S.3    Kitaoka, M.4    Hayashi, K.5
  • 7
    • 0029774346 scopus 로고    scopus 로고
    • Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes
    • Liebl W, Rulie P, Bronnenmeier K, Riedel K, Lottspeich F & Greif I, Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes, Microbiology, 142 (1996) 2533-2542.
    • (1996) Microbiology , vol.142 , pp. 2533-2542
    • Liebl, W.1    Rulie, P.2    Bronnenmeier, K.3    Riedel, K.4    Lottspeich, F.5    Greif, I.6
  • 8
    • 0025772933 scopus 로고
    • Properties of a thermoactive β-1,3-1,4-glucanase (Lichenase) from Clostridium thermocellum expressed in Escherichia coli
    • Schimming S, Schwarz W H & Staudenbauer W L, Properties of a thermoactive β-1,3-1,4-glucanase (Lichenase) from Clostridium thermocellum expressed in Escherichia coli, Biochem Biophys Res Commun, 177 (1991) 447-452.
    • (1991) Biochem Biophys Res Commun , vol.177 , pp. 447-452
    • Schimming, S.1    Schwarz, W.H.2    Staudenbauer, W.L.3
  • 9
    • 0034731485 scopus 로고    scopus 로고
    • Bacterial 1,3-1,4- β-glucanases: Structure, function and protein engineering
    • Planas A, Bacterial 1,3-1,4- β-glucanases: Structure, function and protein engineering, Biochim Biophys Acta, 1543 (2000) 361-382.
    • (2000) Biochim Biophys Acta , vol.1543 , pp. 361-382
    • Planas, A.1
  • 10
    • 0025819512 scopus 로고
    • Molecular cloning, expression and nucleotide sequence of the endo-β-1,3-1,4-D-glucanase gene from Bacillus licheniformis. Predictive structural analyses of the encoded polypeptide
    • Lloberas J, Perez-Pons J A & Querol E, Molecular cloning, expression and nucleotide sequence of the endo-β-1,3-1,4-D-glucanase gene from Bacillus licheniformis. Predictive structural analyses of the encoded polypeptide, Eur J Biochem, 197 (1991) 337-343.
    • (1991) Eur J Biochem , vol.197 , pp. 337-343
    • Lloberas, J.1    Perez-Pons, J.A.2    Querol, E.3
  • 11
    • 0027772710 scopus 로고
    • Stereochemical course and structure of the products of the enzymic action of endo-1,3-1,4-β-D-glucan 4-glucanohydrolase from Bacillus licheniformis
    • Malet C, Jimenez-barbero J, Bernabe M, Brosa C & Planas A, Stereochemical course and structure of the products of the enzymic action of endo-1,3-1,4-β-D-glucan 4-glucanohydrolase from Bacillus licheniformis, Biochem J, 296 (1993) 753-758.
    • (1993) Biochem J , vol.296 , pp. 753-758
    • Malet, C.1    Jimenez-barbero, J.2    Bernabe, M.3    Brosa, C.4    Planas, A.5
  • 12
    • 0016611070 scopus 로고
    • A new substrate for investigating the specificity of β-glucan hydrolases
    • Anderson M A & Stone B A, A new substrate for investigating the specificity of β-glucan hydrolases, FEBS Lett, 52 (1975) 202-207.
    • (1975) FEBS Lett , vol.52 , pp. 202-207
    • Anderson, M.A.1    Stone, B.A.2
  • 13
    • 0001140547 scopus 로고
    • Preparation and properties of a β-D-glucanase for the specific hydrolysis of β-D-glucans
    • Huber D J & Nevins D J, Preparation and properties of a β-D-glucanase for the specific hydrolysis of β-D-glucans, Plant Physiol, 60 (1977) 300-304.
    • (1977) Plant Physiol , vol.60 , pp. 300-304
    • Huber, D.J.1    Nevins, D.J.2
  • 14
    • 0002832135 scopus 로고
    • Molecular characterization of cereal β-D-glucans. Structural analysis of oat β-D-glucan and structural evaluations of β-D-glucans from different sources by high performance liquid chromotagraphy of oligosaccharides released by lichenase
    • Wood D J, Weisz J & Blackwell B A, Molecular characterization of cereal β-D-glucans. Structural analysis of oat β-D-glucan and structural evaluations of β-D-glucans from different sources by high performance liquid chromotagraphy of oligosaccharides released by lichenase, Cereal Chem, 68 (1991b) 31-39.
    • (1991) Cereal Chem , vol.68 , pp. 31-39
    • Wood, D.J.1    Weisz, J.2    Blackwell, B.A.3
  • 15
    • 49049126040 scopus 로고
    • Water-soluble 1,3-, 1,4-β-D-glucans from barley (Hordeum vulgare) endosperm. I. Physicochemical properties
    • Woodward J R, Fincher G B & Stone B A, Water-soluble 1,3-, 1,4-β-D-glucans from barley (Hordeum vulgare) endosperm. I. Physicochemical properties, Carbohydr Polym, 3 (1983) 143-156.
    • (1983) Carbohydr Polym , vol.3 , pp. 143-156
    • Woodward, J.R.1    Fincher, G.B.2    Stone, B.A.3
  • 16
    • 0017083431 scopus 로고
    • Degradation of barley glucan and lichenan by a Bacillus pumilis enzyme
    • Suzuki H & Kaneko T, Degradation of barley glucan and lichenan by a Bacillus pumilis enzyme, Agric Biol Chem, 40 (1976) 577-586.
    • (1976) Agric Biol Chem , vol.40 , pp. 577-586
    • Suzuki, H.1    Kaneko, T.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U K, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature (Lond), 227 (1970) 680-685.
    • (1970) Nature (Lond) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • Somogyi M, Notes on sugar determination, J Biol Chem, 195 (1952) 19-23.
    • (1952) J Biol Chem , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 19
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H & Burk D, The determination of enzyme dissociation constants, J Am Chem Soc, 56 (1934) 658-666.
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 20
    • 0030451399 scopus 로고    scopus 로고
    • Fine substrate specificities of four exo-type cellulases produced by Aspergillus niger, Trichoderma reesei, and Irpex lacteus on 1,3-, 1,4-β-D-glucans and xyloglucan
    • Amano Y, Shroishi M, Nisizawa K, Hoshino E & Kanda T, Fine substrate specificities of four exo-type cellulases produced by Aspergillus niger, Trichoderma reesei, and Irpex lacteus on 1,3-, 1,4-β-D-glucans and xyloglucan, J Biochem (Tokyo), 120 (1996) 1123-1129.
    • (1996) J Biochem (Tokyo) , vol.120 , pp. 1123-1129
    • Amano, Y.1    Shroishi, M.2    Nisizawa, K.3    Hoshino, E.4    Kanda, T.5
  • 21
    • 0000836003 scopus 로고
    • Synthesis of laminarioligosaccharides using a crude extract of Euglena gracilis Z cells
    • Kitaoka M, Sasaki T & Taniguchi H, Synthesis of laminarioligosaccharides using a crude extract of Euglena gracilis Z cells, Agric Biol Chem, 55 (1991) 1431-1432.
    • (1991) Agric Biol Chem , vol.55 , pp. 1431-1432
    • Kitaoka, M.1    Sasaki, T.2    Taniguchi, H.3
  • 22
    • 0027222134 scopus 로고
    • Purification and properties of laminaribiose phosphorylase (EC 2.4.1.31) from Euglena gracilis Z
    • Kitaoka M, Sasaki T & Taniguchi H, Purification and properties of laminaribiose phosphorylase (EC 2.4.1.31) from Euglena gracilis Z, Arch Biochem Biophys, 304 (1993) 508-514.
    • (1993) Arch Biochem Biophys , vol.304 , pp. 508-514
    • Kitaoka, M.1    Sasaki, T.2    Taniguchi, H.3
  • 23
    • 0010018536 scopus 로고    scopus 로고
    • Cellodextrin phosphorylase from Clostridium thermocellum YM4 strain expressed in Escherichia coli
    • Krishnareddy M, Kim Y K, Kitaoka M, Mori Y & Hayashi K, Cellodextrin phosphorylase from Clostridium thermocellum YM4 strain expressed in Escherichia coli, J Appl Glycosci, 49 (2002) 1-8.
    • (2002) J Appl Glycosci , vol.49 , pp. 1-8
    • Krishnareddy, M.1    Kim, Y.K.2    Kitaoka, M.3    Mori, Y.4    Hayashi, K.5
  • 24
    • 0014689999 scopus 로고
    • Purification and properties of β-1,4-oligoglucan:orthophosphate glucosyltransferase from Clostridium thermocellum
    • Sheth K & Alexander J K, Purification and properties of β-1,4-oligoglucan:orthophosphate glucosyltransferase from Clostridium thermocellum, J Biol Chem, 244 (1969) 457-464.
    • (1969) J Biol Chem , vol.244 , pp. 457-464
    • Sheth, K.1    Alexander, J.K.2
  • 25
    • 0025316285 scopus 로고
    • The Glu residue in the conserved Asn-Glu-Pro sequence of two highly divergent endo- β-1,4-glucanases is essential for enzyme activity
    • Baird S D, Hefford M A, Johnson D A, Sung W L, Yaguchi M & Seligy V L, The Glu residue in the conserved Asn-Glu-Pro sequence of two highly divergent endo- β-1,4-glucanases is essential for enzyme activity, Biochem Biophys Res Commun, 169 (1990) 1035-1039.
    • (1990) Biochem Biophys Res Commun , vol.169 , pp. 1035-1039
    • Baird, S.D.1    Hefford, M.A.2    Johnson, D.A.3    Sung, W.L.4    Yaguchi, M.5    Seligy, V.L.6
  • 26
    • 0028207101 scopus 로고
    • Cloning and DNA sequencing of bgaA, a gene encoding an endo-β-1,3-1,4- glucanase from an alkalophilic Bacillus strain (N137)
    • Tabernero C, Coll P M, Fernandez-Abalos J M, Perez P & Santamaria R I, Cloning and DNA sequencing of bgaA, a gene encoding an endo-β-1,3-1,4- glucanase from an alkalophilic Bacillus strain (N137), Appl Environ Microbiol, 60 (1994) 1213-1220.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1213-1220
    • Tabernero, C.1    Coll, P.M.2    Fernandez-Abalos, J.M.3    Perez, P.4    Santamaria, R.I.5
  • 27
    • 0030883632 scopus 로고    scopus 로고
    • Sequencing of a 1,3-1,4-β-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, Li X L & Ljungdahl L G, Sequencing of a 1,3-1,4-β-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 (1997) 6028-6034.
    • (1997) J Bacteriol , vol.179 , pp. 6028-6034
    • Chen, H.1    Li, X.L.2    Ljungdahl, L.G.3
  • 28
    • 0034575297 scopus 로고    scopus 로고
    • Molecular weight, structure, and shape of oat 1,3- 1,4-β-D-glucan fractions obtained by enzymatic degradation with lichenase
    • Roubroeks J P, Mastromauro D I, Andersson R, Christensen B E & Aman P, Molecular weight, structure, and shape of oat 1,3- 1,4-β-D-glucan fractions obtained by enzymatic degradation with lichenase, Biomacromol, 1 (2000) 584-591.
    • (2000) Biomacromol , vol.1 , pp. 584-591
    • Roubroeks, J.P.1    Mastromauro, D.I.2    Andersson, R.3    Christensen, B.E.4    Aman, P.5
  • 29
    • 0033957024 scopus 로고    scopus 로고
    • A transglycosylating 1,3(4)-β-glucanase from Rhodothermus marinus NMR analysis of enzyme reactions
    • Petersen B O, Krah M, Duus J O & Thomsen K K, A transglycosylating 1,3(4)-β-glucanase from Rhodothermus marinus NMR analysis of enzyme reactions, Eur J Biochem, 267 (2000) 361-369.
    • (2000) Eur J Biochem , vol.267 , pp. 361-369
    • Petersen, B.O.1    Krah, M.2    Duus, J.O.3    Thomsen, K.K.4
  • 30
    • 0025876050 scopus 로고
    • Nucleotide sequence and characteristics of endoglucanase gene engB from Clostridium cellulovorans
    • Foong F, Hamamoto T, Shoseyov O & Doi R H, Nucleotide sequence and characteristics of endoglucanase gene engB from Clostridium cellulovorans, J Gen Microbiol, 137 (1991) 1729-1736.
    • (1991) J Gen Microbiol , vol.137 , pp. 1729-1736
    • Foong, F.1    Hamamoto, T.2    Shoseyov, O.3    Doi, R.H.4


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