메뉴 건너뛰기




Volumn 21, Issue 1, 1998, Pages 1-11

Properties of an α-galactosidase, and structure of its gene galA, within an α- and β-galactoside utilization gene cluster of the hyperthermophilic bacterium thermotoga maritima

Author keywords

Alpha galactosidase; Beta galactosidase thermostability; galA; galK; galT; lacZ; Nucleotide sequence; Raffinose hydrolysis

Indexed keywords

4 NITROPHENYLGALACTOSIDE; ALPHA GALACTOSIDASE; BACTERIAL ENZYME; BETA GALACTOSIDE; GALACTOKINASE; GALACTOSE; GALACTOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; MELIBIOSE; RAFFINOSE; RECOMBINANT PROTEIN;

EID: 0031894595     PISSN: 07232020     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0723-2020(98)80002-7     Document Type: Article
Times cited : (40)

References (40)
  • 1
    • 0025862986 scopus 로고
    • Biochemical and genetic analysis of Streptococcus mutans α-galactosidase
    • ADUSE-OPOKU, J., TAO, L., FERRETTI, J. J., RUSSELL, R. B. B.: Biochemical and genetic analysis of Streptococcus mutans α-galactosidase. J. Gen. Microbiol. 137, 757-764 (1991).
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 757-764
    • Aduse-Opoku, J.1    Tao, L.2    Ferretti, J.J.3    Russell, R.B.B.4
  • 2
    • 0001446166 scopus 로고
    • Regioselective synthesis of trisaccharides by use of a reversed hydrolysis of α- and β-galactosidase
    • AJISAKA, K., FUJIMOTO, H.: Regioselective synthesis of trisaccharides by use of a reversed hydrolysis of α- and β-galactosidase. Carbohydr. Res. 185, 139-146 (1989).
    • (1989) Carbohydr. Res. , vol.185 , pp. 139-146
    • Ajisaka, K.1    Fujimoto, H.2
  • 4
    • 0015240654 scopus 로고
    • The α-galactosidase from Escherichia coli K12
    • BURSTEIN, C., KEPES, A.: The α-galactosidase from Escherichia coli K12. Biochim Biophys. Acta 230, 52-63 (1971).
    • (1971) Biochim Biophys. Acta , vol.230 , pp. 52-63
    • Burstein, C.1    Kepes, A.2
  • 5
    • 0029391545 scopus 로고
    • The DAG family of glycosyl hydrolases combines two previously identified protein families
    • DAGNALL, B. H., PAULSEN, I. T., SAIER, M. H.: The DAG family of glycosyl hydrolases combines two previously identified protein families. Biochem. J. 311, 349-350 (1995).
    • (1995) Biochem. J. , vol.311 , pp. 349-350
    • Dagnall, B.H.1    Paulsen, I.T.2    Saier, M.H.3
  • 6
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • DEVEREUX, J., HAEBERLI, P., SMITHIES, O.: A comprehensive set of sequence analysis programs for the VAX. Nucl. Acids. Res. 12, 387-395 (1984).
    • (1984) Nucl. Acids. Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 7
    • 0031023550 scopus 로고    scopus 로고
    • Purification and characterization of extremely thermostable β-mannanase, β-mannosidase, and α-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068
    • DUFFAUD, G. D., MCCUTCHEN, C. M., LEDUC, P., PARKER, K. N., KELLY, R. M.: Purification and characterization of extremely thermostable β-mannanase, β-mannosidase, and α-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068. Appl. Environ. Microbiol. 63, 169-177 (1997).
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 169-177
    • Duffaud, G.D.1    Mccutchen, C.M.2    Leduc, P.3    Parker, K.N.4    Kelly, R.M.5
  • 8
    • 84987368356 scopus 로고
    • Purification and characterization of a Clostridium perfringens α-galactosidase
    • DURANCE, T., SKURA, B.: Purification and characterization of a Clostridium perfringens α-galactosidase. J. Food Sci. 50, 518-522 (1985).
    • (1985) J. Food Sci. , vol.50 , pp. 518-522
    • Durance, T.1    Skura, B.2
  • 9
    • 0027253969 scopus 로고
    • Cloning and characterization of β-galactoside and β-glucoside hydrolysing enzymes of Thermotoga maritima
    • GABELSBERGER, J., LIEBL, W., SCHLEIFER, K. H.: Cloning and characterization of β-galactoside and β-glucoside hydrolysing enzymes of Thermotoga maritima. FEMS Microbiol. Lett. 109, 131-138 (1993).
    • (1993) FEMS Microbiol. Lett. , vol.109 , pp. 131-138
    • Gabelsberger, J.1    Liebl, W.2    Schleifer, K.H.3
  • 10
    • 0024094905 scopus 로고
    • Production of thermostable, recombinant α-galactosidase suitable for raffinose elimination from sugar beet syrup
    • GANTER, C., BÖCK, A., BUCKEL, P., MATTES, R.: Production of thermostable, recombinant α-galactosidase suitable for raffinose elimination from sugar beet syrup. J. Biotechnol. 8, 301-310 (1988).
    • (1988) J. Biotechnol. , vol.8 , pp. 301-310
    • Ganter, C.1    Böck, A.2    Buckel, P.3    Mattes, R.4
  • 12
    • 0029669440 scopus 로고    scopus 로고
    • Purification of α-galactosidase from Lactobacillus fermentum
    • GARRO, M. S., DE VALDEZ, G. F., OLIVER, G., DE GIORI, G. S.: Purification of α-galactosidase from Lactobacillus fermentum. J. Biotechnol. 45, 103-109 (1996).
    • (1996) J. Biotechnol. , vol.45 , pp. 103-109
    • Garro, M.S.1    De Valdez, G.F.2    Oliver, G.3    De Giori, G.S.4
  • 14
    • 84954865637 scopus 로고
    • Purification and some properties of α-galactosidase from Pseudomonas fluorescens H-601
    • HASHIMOTO, H., GOTO, M., KATAYAMA, C., KITAHATA, S.: Purification and some properties of α-galactosidase from Pseudomonas fluorescens H-601. Biosci. Biotech. Biochem. 55, 2831-2838 (1991).
    • (1991) Biosci. Biotech. Biochem. , vol.55 , pp. 2831-2838
    • Hashimoto, H.1    Goto, M.2    Katayama, C.3    Kitahata, S.4
  • 15
    • 0000049352 scopus 로고
    • Purification and some properties of α-galactosidase from Candida guillermondii H-404
    • HASHIMOTO, H., KATAYAMA, C., GOTO, M., KITAHATA, S.: Purification and some properties of α-galactosidase from Candida guillermondii H-404. Biosci. Biotech. Biochem. 57, 372-378 (1993).
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 372-378
    • Hashimoto, H.1    Katayama, C.2    Goto, M.3    Kitahata, S.4
  • 16
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • HENRISSAT, B.: A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280, 309-316 (1991).
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 17
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • HENRISSAT, B., BAIROCH, A.: New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293, 781-788 (1993).
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 18
    • 0024598146 scopus 로고
    • Fast and sensitive multiple sequence alignment on a microcomputer
    • HIGGINS, D. G., SHARP, P. M.: Fast and sensitive multiple sequence alignment on a microcomputer. CABIOS 5, 151-153 (1989).
    • (1989) CABIOS , vol.5 , pp. 151-153
    • Higgins, D.G.1    Sharp, P.M.2
  • 19
    • 0001846919 scopus 로고
    • The order Thermotogales
    • (A. BALOWS, H. G. TRÜPER, M. DWORKIN, W. HARDER, K. H. SCHLEIFER, eds.). 2nd ed., Springer-Verlag, New York
    • HUBER, R., STETTER, K. O.: The order Thermotogales, pp. 3809-3815. In: The Procaryotes (A. BALOWS, H. G. TRÜPER, M. DWORKIN, W. HARDER, K. H. SCHLEIFER, eds.). Vol. IV, 2nd ed., Springer-Verlag, New York 1992.
    • (1992) The Procaryotes , vol.4 , pp. 3809-3815
    • Huber, R.1    Stetter, K.O.2
  • 20
    • 0025336553 scopus 로고
    • Cloning of α- and β-galactosidase genes from an extreme thermophile, Thermus strain T2, and their expression in Thermus thermophilus HB27
    • KOYAMA, Y., OKAMOTO, S., FURUKAWA, K.: Cloning of α- and β-galactosidase genes from an extreme thermophile, Thermus strain T2, and their expression in Thermus thermophilus HB27. Appl. Environ. Microbiol. 56, 2251-2254 (1990).
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 2251-2254
    • Koyama, Y.1    Okamoto, S.2    Furukawa, K.3
  • 21
    • 0026660023 scopus 로고
    • Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli
    • LIEBL, W., FEIL, R., GABELSBERGER, J., KELLERMANN, J., SCHLEIFER, K. H.: Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli. Eur J. Biochem. 207, 81-88 (1992).
    • (1992) Eur J. Biochem. , vol.207 , pp. 81-88
    • Liebl, W.1    Feil, R.2    Gabelsberger, J.3    Kellermann, J.4    Schleifer, K.H.5
  • 22
    • 0028123353 scopus 로고
    • Comparative amino sequence analysis of Thermotoga maritima β-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between β-glucosidases of the BGA family and other families of β-1,4-glycosyl hydrolases
    • LIEBL, W., GABELSBERGER, J., SCHLEIFER, K. H.: Comparative amino sequence analysis of Thermotoga maritima β-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between β-glucosidases of the BGA family and other families of β-1,4-glycosyl hydrolases. Mol. Gen. Genet. 242, 111-115 (1994).
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 111-115
    • Liebl, W.1    Gabelsberger, J.2    Schleifer, K.H.3
  • 23
    • 0031028407 scopus 로고    scopus 로고
    • Properties and gene structure of the Thermotoga maritima α-amylase AmyA, a putative lipoprotein of a hyperthermophilic bacterium
    • LIEBL, W., STEMPLINGER, I., RUILE, P.: Properties and gene structure of the Thermotoga maritima α-amylase AmyA, a putative lipoprotein of a hyperthermophilic bacterium. J. Bacteriol., 179, 941-948 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 941-948
    • Liebl, W.1    Stemplinger, I.2    Ruile, P.3
  • 24
    • 0029847258 scopus 로고    scopus 로고
    • Three α-galactosidase genes of Trichoderma reesei cloned by expression in yeast
    • MARGOLLES-CLARK, E., TENKANEN, M., LUONTERI, E., PENTTILÄ, M.: Three α-galactosidase genes of Trichoderma reesei cloned by expression in yeast. Eur. J. Biochem. 240, 104-111 (1996).
    • (1996) Eur. J. Biochem. , vol.240 , pp. 104-111
    • Margolles-Clark, E.1    Tenkanen, M.2    Luonteri, E.3    Penttilä, M.4
  • 25
    • 10144234125 scopus 로고    scopus 로고
    • Characterization of extremely thermostable enzymatic breakers (α-1,6-galactosidase and β-mannanase) from the hyperthermophilic bacterium Thermotoga neapolitana 5068 for hydrolysis of guar gum
    • MCCUTCHEN, C. M., DUFFAUD, G. D., LEDUC, P., PETERSEN, A. R. H., TAYAL, A., KHAN, S. A., KELLY, R. M.: Characterization of extremely thermostable enzymatic breakers (α-1,6-galactosidase and β-mannanase) from the hyperthermophilic bacterium Thermotoga neapolitana 5068 for hydrolysis of guar gum. Biotechnol. Bioeng. 52, 332-339 (1996).
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 332-339
    • Mccutchen, C.M.1    Duffaud, G.D.2    Leduc, P.3    Petersen, A.R.H.4    Tayal, A.5    Khan, S.A.6    Kelly, R.M.7
  • 26
    • 0028065197 scopus 로고
    • Identification and sequencing of the Thermotoga maritima lacZ gene, part of a divergently transcribed operon
    • MOORE, J. B., MARKIEWICZ, P., MILLER, J. H.: Identification and sequencing of the Thermotoga maritima lacZ gene, part of a divergently transcribed operon. Gene 147, 101-106 (1994).
    • (1994) Gene , vol.147 , pp. 101-106
    • Moore, J.B.1    Markiewicz, P.2    Miller, J.H.3
  • 27
    • 0026742336 scopus 로고
    • Characterization of alpha-galactosidase from Corynebacterium murisepticum and mechanism of its induction
    • NADKARNI, M. A., NAIR, C. K. K., PANDEY, V. N., PRADHAN D. S.: Characterization of alpha-galactosidase from Corynebacterium murisepticum and mechanism of its induction. J. Gen. Appl. Microbiol. 38, 23-34 (1992).
    • (1992) J. Gen. Appl. Microbiol. , vol.38 , pp. 23-34
    • Nadkarni, M.A.1    Nair, C.K.K.2    Pandey, V.N.3    Pradhan, D.S.4
  • 28
    • 0027524560 scopus 로고
    • The L-lactate dehydrogenase gene of the hyperthermophilic bacterium Thermotoga maritima cloned by complementation in Escherichia coli
    • OSTENDORP, R., LIEBL, W., SCHURIG, H., JAENICKE, R.: The L-lactate dehydrogenase gene of the hyperthermophilic bacterium Thermotoga maritima cloned by complementation in Escherichia coli. Eur. J. Biochem. 216, 709-715 (1993).
    • (1993) Eur. J. Biochem. , vol.216 , pp. 709-715
    • Ostendorp, R.1    Liebl, W.2    Schurig, H.3    Jaenicke, R.4
  • 30
    • 0027292499 scopus 로고
    • Purification and molecular properties of an α-galactosidase synthesized and secreted by Aspergillus nidulans
    • RIOS, S., PEDREGOSA, A. M., MONISTROL, I. F., LABORDA, F.: Purification and molecular properties of an α-galactosidase synthesized and secreted by Aspergillus nidulans. FEMS Microbiol. Lett. 112, 35-42 (1993).
    • (1993) FEMS Microbiol. Lett. , vol.112 , pp. 35-42
    • Rios, S.1    Pedregosa, A.M.2    Monistrol, I.F.3    Laborda, F.4
  • 31
    • 0017073611 scopus 로고
    • Raffinose metabilism in Escherichia coli K12
    • SCHMID, K., SCHMITT, R.: Raffinose metabilism in Escherichia coli K12. Eur. J. Biochem. 67, 95-104 (1976).
    • (1976) Eur. J. Biochem. , vol.67 , pp. 95-104
    • Schmid, K.1    Schmitt, R.2
  • 32
    • 0022423417 scopus 로고
    • Deletion of C-terminal amino acid codons of PhiX174 gene E: Effect on its lysis inducing properties
    • SCHÜLLER, A., HARKNESS, R. E., RÜTHER, U., LUBITZ, W.: Deletion of C-terminal amino acid codons of PhiX174 gene E: effect on its lysis inducing properties. Nucl. Acids Res. 13, 4143-4152 (1985).
    • (1985) Nucl. Acids Res. , vol.13 , pp. 4143-4152
    • Schüller, A.1    Harkness, R.E.2    Rüther, U.3    Lubitz, W.4
  • 33
    • 0028356024 scopus 로고
    • 2 in the anaerobic hyperthermophilic eubacterium Thermotoga maritima: Involvement of the Embden-Meyerhof pathway
    • 2 in the anaerobic hyperthermophilic eubacterium Thermotoga maritima: involvement of the Embden-Meyerhof pathway. Arch. Microbiol. 161, 460-470 (1994).
    • (1994) Arch. Microbiol. , vol.161 , pp. 460-470
    • Schröder, C.1    Selig, M.2    Schönheit, P.3
  • 34
    • 0029991767 scopus 로고    scopus 로고
    • Hyperthermophilic procaryotes
    • STETTER, K. O.: Hyperthermophilic procaryotes. FEMS Microbiol. Rev. 18, 149-158 (1996).
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 149-158
    • Stetter, K.O.1
  • 35
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • STUDIER, F. W., MOFFATT, B. A.: Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130 (1986).
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 36
    • 0025002095 scopus 로고
    • Purification and characterization of thermostable β-mannanase and α-galactosidase from Bacillus stearothermophilus
    • TALBOT, G., SYGUSCH, J.: Purification and characterization of thermostable β-mannanase and α-galactosidase from Bacillus stearothermophilus. Appl. Environ. Microbiol. 56, 3505-3510 (1990).
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3505-3510
    • Talbot, G.1    Sygusch, J.2
  • 37
    • 0029008857 scopus 로고
    • Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima strain MSB8
    • WINTERHALTER, C., LIEBL, W.: Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima strain MSB8. Appl. Environ. Microbiol. 61, 1810-1815 (1995).
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1810-1815
    • Winterhalter, C.1    Liebl, W.2
  • 38
    • 0028901697 scopus 로고
    • Identification of a novel cellulose-binding domain within the multi-domain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima
    • WINTERHALTER, C., HEINRICH, P., CANDUSSIO, A., WICH, G., LIEBL, W.: Identification of a novel cellulose-binding domain within the multi-domain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima. Mol. Microbiol. 15, 431-444 (1995).
    • (1995) Mol. Microbiol. , vol.15 , pp. 431-444
    • Winterhalter, C.1    Heinrich, P.2    Candussio, A.3    Wich, G.4    Liebl, W.5
  • 39
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequence of the M13mp18 and pUC vectors
    • YANISH-PERON, C., VIEIRA, J., MESSING, J.: Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mp18 and pUC vectors. Gene 33, 103-119 (1985).
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanish-Peron, C.1    Vieira, J.2    Messing, J.3
  • 40
    • 0027287853 scopus 로고
    • Conditions of formation, purification, and characterization of an α-galactosidase of Trichoderma reesei RUT C-30
    • ZEILINGER, S., KRISTUFEK, D., ARISAN-ATAC, I., HODITS, R., KUBICEK, C. P.: Conditions of formation, purification, and characterization of an α-galactosidase of Trichoderma reesei RUT C-30. Appl. Environ. Microbiol. 59, 1347-1353 (1993).
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1347-1353
    • Zeilinger, S.1    Kristufek, D.2    Arisan-Atac, I.3    Hodits, R.4    Kubicek, C.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.