메뉴 건너뛰기




Volumn 37, Issue 5, 2005, Pages 472-480

Purification and characterization of the hyper-glycosylated extracellular α-glucosidase from Schizosaccharomyces pombe

Author keywords

Glucosidase; Glycoside hydrolase family 31; Hyper glycosylated enzyme; Schizosaccharomyces pombe

Indexed keywords

ENZYMES; MAGNETIC SUSCEPTIBILITY; MOLECULAR BIOLOGY; PROTEINS; PURIFICATION; SUBSTRATES; SUGAR (SUCROSE);

EID: 23744447380     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2004.06.018     Document Type: Article
Times cited : (30)

References (46)
  • 2
    • 0031201675 scopus 로고    scopus 로고
    • Molecular mechanism in alpha-glucosidase and glucoamylase
    • S. Chiba Molecular mechanism in alpha-glucosidase and glucoamylase Biosci Biotechnol Biochem 61 1997 1233 1239
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1233-1239
    • Chiba, S.1
  • 3
    • 0031972297 scopus 로고    scopus 로고
    • Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin
    • T.P. Frandsen, and B. Svensson Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin Plant Mol Biol 37 1998 1 13
    • (1998) Plant Mol Biol , vol.37 , pp. 1-13
    • Frandsen, T.P.1    Svensson, B.2
  • 4
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat A classification of glycosyl hydrolases based on amino acid sequence similarities Biochem J 280 1991 309 316
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 5
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat, and A. Bairoch New families in the classification of glycosyl hydrolases based on amino acid sequence similarities Biochem J 293 1993 781 788
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 6
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • B. Henrissat, and G. Davies Structural and sequence-based classification of glycoside hydrolases Curr Opin Struct Biol 7 1997 637 644
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 7
    • 0035006850 scopus 로고    scopus 로고
    • Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe
    • M. Okuyama, A. Okuno, N. Shimizu, H. Mori, A. Kimura, and S. Chiba Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe Eur J Biochem 268 2001 2270 2280
    • (2001) Eur J Biochem , vol.268 , pp. 2270-2280
    • Okuyama, M.1    Okuno, A.2    Shimizu, N.3    Mori, H.4    Kimura, A.5    Chiba, S.6
  • 8
    • 84954871548 scopus 로고
    • Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger
    • A. Kita, H. Matsui, A. Somoto, A. Kimura, M. Takata, and S. Chiba Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger Agric Biol Chem 55 1991 2327 2335
    • (1991) Agric Biol Chem , vol.55 , pp. 2327-2335
    • Kita, A.1    Matsui, H.2    Somoto, A.3    Kimura, A.4    Takata, M.5    Chiba, S.6
  • 9
    • 0017821899 scopus 로고
    • Purification and properties of an α-glucosidase (glucoamylase) in sugar beet seed
    • S. Chiba, S. Inomata, H. Matsui, and T. Shimomura Purification and properties of an α-glucosidase (glucoamylase) in sugar beet seed Agric Biol Chem 42 1978 241 245
    • (1978) Agric Biol Chem , vol.42 , pp. 241-245
    • Chiba, S.1    Inomata, S.2    Matsui, H.3    Shimomura, T.4
  • 10
    • 0034126439 scopus 로고    scopus 로고
    • Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point α-glucosidase from barley malt
    • T.P. Frandsen, F. Lok, E. Mirgorodskaya, P. Roepstorff, and B. Svensson Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point α-glucosidase from barley malt Plant Physiol 123 2000 275 286
    • (2000) Plant Physiol , vol.123 , pp. 275-286
    • Frandsen, T.P.1    Lok, F.2    Mirgorodskaya, E.3    Roepstorff, P.4    Svensson, B.5
  • 11
    • 0028886770 scopus 로고
    • Characterization of high pI α-glucosidase from germinated barley seeds: Substrate specificity, subsite affinities and active-site residues
    • H. Im, and C.A. Henson Characterization of high pI α-glucosidase from germinated barley seeds: substrate specificity, subsite affinities and active-site residues Carbohydr Res 277 1995 145 159
    • (1995) Carbohydr Res , vol.277 , pp. 145-159
    • Im, H.1    Henson, C.A.2
  • 12
    • 0028852767 scopus 로고
    • Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus
    • M. Rolfsmeier, and P. Blum Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus J Bacteriol 177 1995 482 485
    • (1995) J Bacteriol , vol.177 , pp. 482-485
    • Rolfsmeier, M.1    Blum, P.2
  • 13
    • 0022017193 scopus 로고
    • Purification and characterization of lysosomal α-glucosidase secreted by eukaryote Tetrahymena
    • Y. Banno, and Y. Nozawa Purification and characterization of lysosomal α-glucosidase secreted by eukaryote Tetrahymena J Biochem (Tokyo) 97 1985 409 418
    • (1985) J Biochem (Tokyo) , vol.97 , pp. 409-418
    • Banno, Y.1    Nozawa, Y.2
  • 14
    • 0022342288 scopus 로고
    • Purification and some properties of lysosomal α-glucosidase of rat liver
    • R. Scheibe, K.W. Wenzel, and E. Hofmann Purification and some properties of lysosomal α-glucosidase of rat liver Biomed Biochim Acta 44 1985 1279 1286
    • (1985) Biomed Biochim Acta , vol.44 , pp. 1279-1286
    • Scheibe, R.1    Wenzel, K.W.2    Hofmann, E.3
  • 15
    • 0022580798 scopus 로고
    • Isolation and characterization of three α-glucosidases from the Japanese quail
    • F. Usuki, S. Ishiura, and H. Sugita Isolation and characterization of three α-glucosidases from the Japanese quail J Biochem (Tokyo) 99 1986 985 988
    • (1986) J Biochem (Tokyo) , vol.99 , pp. 985-988
    • Usuki, F.1    Ishiura, S.2    Sugita, H.3
  • 16
    • 0014952621 scopus 로고
    • Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme
    • P.L. Jeffrey, D.H. Brown, and B.I. Brown Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme Biochemistry 9 1970 1403 1415
    • (1970) Biochemistry , vol.9 , pp. 1403-1415
    • Jeffrey, P.L.1    Brown, D.H.2    Brown, B.I.3
  • 18
    • 0028466976 scopus 로고
    • Calculation of subsite affinities of human small intestinal glucoamylase-maltase
    • H. Heymann, and S. Gunther Calculation of subsite affinities of human small intestinal glucoamylase-maltase Biol Chem Hoppe Seyler 375 1994 451 455
    • (1994) Biol Chem Hoppe Seyler , vol.375 , pp. 451-455
    • Heymann, H.1    Gunther, S.2
  • 19
    • 0016750245 scopus 로고
    • Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits
    • K.A. Conklin, K.M. Yamashiro, and G.M. Gray Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits J Biol Chem 250 1975 5735 5741
    • (1975) J Biol Chem , vol.250 , pp. 5735-5741
    • Conklin, K.A.1    Yamashiro, K.M.2    Gray, G.M.3
  • 20
    • 0015516320 scopus 로고
    • Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine
    • J. Kolinska, and J. Kraml Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine Biochim Biophys Acta 284 1972 235 247
    • (1972) Biochim Biophys Acta , vol.284 , pp. 235-247
    • Kolinska, J.1    Kraml, J.2
  • 21
    • 0031001295 scopus 로고    scopus 로고
    • r 540,000 homohexameric α-glucosidase with both exo-α-l,4-glucosidase and oligo-l, 6-glucosidase activities
    • r 540,000 homohexameric α-glucosidase with both exo-α-l,4-glucosidase and oligo-l, 6-glucosidase activities Eur J Biochem 245 1997 129 136
    • (1997) Eur J Biochem , vol.245 , pp. 129-136
    • Suzuki, Y.1    Nobiki, M.2    Matsuda, M.3    Sawai, T.4
  • 22
    • 15144341062 scopus 로고    scopus 로고
    • α-Glucosidase from the hepatopancreas of the shrimp. Penaeus vannamei (Crustacea-Decapoda)
    • P. Le Chevalier, and A. Van Wormhoudt α-Glucosidase from the hepatopancreas of the shrimp. Penaeus vannamei (Crustacea-Decapoda) J Exp Zool 280 1998 384 394
    • (1998) J Exp Zool , vol.280 , pp. 384-394
    • Le Chevalier, P.1    Van Wormhoudt, A.2
  • 23
    • 0029281599 scopus 로고
    • Human small intestinal sucrase-isomaltase: Different binding patterns for malto- and isomaltooligosaccharides
    • H. Heymann, D. Breitmeier, and S. Gunther Human small intestinal sucrase-isomaltase: different binding patterns for malto- and isomaltooligosaccharides Biol Chem Hoppe Seyler 376 1995 249 253
    • (1995) Biol Chem Hoppe Seyler , vol.376 , pp. 249-253
    • Heymann, H.1    Breitmeier, D.2    Gunther, S.3
  • 24
    • 0028890556 scopus 로고
    • Multiple molecular forms of α-glucosidase from spinach seeds, Spnacia oleracea L
    • M. Sugimoto, S. Furui, and Y. Suzuki Multiple molecular forms of α-glucosidase from spinach seeds, Spnacia oleracea L Biosci Biotech Biochem 59 1995 673 677
    • (1995) Biosci Biotech Biochem , vol.59 , pp. 673-677
    • Sugimoto, M.1    Furui, S.2    Suzuki, Y.3
  • 25
    • 0001090256 scopus 로고
    • Subsite affinities of α-glucosidase from Mucor javanicus
    • M. Sugimoto, and Y. Suzuki Subsite affinities of α-glucosidase from Mucor javanicus Biosci Biotech Biochem 57 1993 1378 1379
    • (1993) Biosci Biotech Biochem , vol.57 , pp. 1378-1379
    • Sugimoto, M.1    Suzuki, Y.2
  • 26
    • 0007553835 scopus 로고
    • Substrate specificity of an α-glucosidase in sugar beet seed
    • H. Matsui, S. Chiba, and T. Shimomura Substrate specificity of an α-glucosidase in sugar beet seed Agric Biol Chem 42 1978 1855 1860
    • (1978) Agric Biol Chem , vol.42 , pp. 1855-1860
    • Matsui, H.1    Chiba, S.2    Shimomura, T.3
  • 27
    • 0000689227 scopus 로고
    • A xyloglucan-oligosaccharide-specific α-d-xylosidase or exo-oligoxyloglucan-α-xylohydrolase from germinated nasturtium (Tropeaolum majus L.) seeds
    • C. Fanutti, M.J. Gidley, and J.S. Grant-Reid A xyloglucan- oligosaccharide-specific α-d-xylosidase or exo-oligoxyloglucan-α- xylohydrolase from germinated nasturtium (Tropeaolum majus L.) seeds Planta 184 1991 137 147
    • (1991) Planta , vol.184 , pp. 137-147
    • Fanutti, C.1    Gidley, M.J.2    Grant-Reid, J.S.3
  • 29
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • M. Dubois, R. Gilles, J.K. Hamilton, P.A. Robers, and F. Smith Colorimetric method for determination of sugars and related substances Anal Chem 28 1956 350 356
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, R.2    Hamilton, J.K.3    Robers, P.A.4    Smith, F.5
  • 30
    • 0001023065 scopus 로고
    • Quantitative study of anomeric forms of glucose produced by α-glucosidase and glucoamylase
    • S. Chiba, A. Kimura, and H. Matsui Quantitative study of anomeric forms of glucose produced by α-glucosidase and glucoamylase Agric Biol Chem 47 1983 1741 1746
    • (1983) Agric Biol Chem , vol.47 , pp. 1741-1746
    • Chiba, S.1    Kimura, A.2    Matsui, H.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0036808537 scopus 로고    scopus 로고
    • FindPept, a tool to identify unmatched masses in peptide mass fingerprinting protein identification
    • A. Gattiker, W.V. Bienvenut, A. Bairoch, and E. Gasteiger FindPept, a tool to identify unmatched masses in peptide mass fingerprinting protein identification Proteomics 2 2002 1435 1444
    • (2002) Proteomics , vol.2 , pp. 1435-1444
    • Gattiker, A.1    Bienvenut, W.V.2    Bairoch, A.3    Gasteiger, E.4
  • 33
    • 0033546122 scopus 로고    scopus 로고
    • High-throughput mass spectrometric discovery of protein post-translational modifications
    • M.R. Wilkins, E. Gasteiger, A.A. Gooley, B.R. Herbert, M.P. Molloy, and P.A. Binz High-throughput mass spectrometric discovery of protein post-translational modifications J Mol Biol 289 1999 645 657
    • (1999) J Mol Biol , vol.289 , pp. 645-657
    • Wilkins, M.R.1    Gasteiger, E.2    Gooley, A.A.3    Herbert, B.R.4    Molloy, M.P.5    Binz, P.A.6
  • 34
    • 0035261661 scopus 로고    scopus 로고
    • GlycoMod - A software tool for determining glycosylation compositions from mass spectrometric data
    • C.A. Cooper, E. Gasteiger, and N. Packer GlycoMod - a software tool for determining glycosylation compositions from mass spectrometric data Proteomics 1 2001 340 349
    • (2001) Proteomics , vol.1 , pp. 340-349
    • Cooper, C.A.1    Gasteiger, E.2    Packer, N.3
  • 35
    • 0015921531 scopus 로고
    • Subsite affinities of glucoamylase: Examination of the validity of the subsite theory
    • K. Hiromi, Y. Nitta, C. Numata, and S. Ono Subsite affinities of glucoamylase: examination of the validity of the subsite theory Biochim Biophys Acta 302 1973 362 375
    • (1973) Biochim Biophys Acta , vol.302 , pp. 362-375
    • Hiromi, K.1    Nitta, Y.2    Numata, C.3    Ono, S.4
  • 36
    • 0014943898 scopus 로고
    • Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exo-enzyme
    • K. Hiromi Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exo-enzyme Biochem Biophys Res Commun 40 1970 1 6
    • (1970) Biochem Biophys Res Commun , vol.40 , pp. 1-6
    • Hiromi, K.1
  • 37
    • 0025974948 scopus 로고
    • Improvement of bacterial β-glucanase thermostability by glycosylation
    • O. Olsen, and K.K. Thomsen Improvement of bacterial β-glucanase thermostability by glycosylation J Gen Microbiol 137 1991 579 585
    • (1991) J Gen Microbiol , vol.137 , pp. 579-585
    • Olsen, O.1    Thomsen, K.K.2
  • 38
    • 0021518752 scopus 로고
    • Role of the carbohydrate part of yeast acid phosphatase
    • S. Barbaric, V. Mrsa, B. Ries, and P. Mildner Role of the carbohydrate part of yeast acid phosphatase Arch Biochem Biophys 234 1984 567 575
    • (1984) Arch Biochem Biophys , vol.234 , pp. 567-575
    • Barbaric, S.1    Mrsa, V.2    Ries, B.3    Mildner, P.4
  • 39
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • C. Wang, M. Eufemi, C. Turano, and A. Giartosio Influence of the carbohydrate moiety on the stability of glycoproteins Biochemistry 35 1996 7299 7307
    • (1996) Biochemistry , vol.35 , pp. 7299-7307
    • Wang, C.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 41
    • 0021112695 scopus 로고
    • Effect of size and location of the oligosaccharide chain on protease degradation of bovine pancreatic ribonuclease
    • B.A. Bernard, S.A. Newton, and K. Olden Effect of size and location of the oligosaccharide chain on protease degradation of bovine pancreatic ribonuclease J Biol Chem 258 1983 12198 12202
    • (1983) J Biol Chem , vol.258 , pp. 12198-12202
    • Bernard, B.A.1    Newton, S.A.2    Olden, K.3
  • 42
    • 0022352978 scopus 로고
    • Subcellular localization and glycoprotein nature of the invertase from the fission yeast Schizosaccharomyces pombe
    • S. Moreno, T. Ruiz, Y. Sanchez, J.R. Villanueva, and L. Rodriguez Subcellular localization and glycoprotein nature of the invertase from the fission yeast Schizosaccharomyces pombe Arch Microbiol 142 1985 370 374
    • (1985) Arch Microbiol , vol.142 , pp. 370-374
    • Moreno, S.1    Ruiz, T.2    Sanchez, Y.3    Villanueva, J.R.4    Rodriguez, L.5
  • 43
    • 0019811892 scopus 로고
    • Isolation, properties, function, and regulation of endo-(l → 3)-β-glucanases in Schizosaccharomyces pombe
    • B.Y. Reichelt, and G.H. Fleet Isolation, properties, function, and regulation of endo-(l → 3)-β-glucanases in Schizosaccharomyces pombe J Bacteriol 147 1981 1085 1094
    • (1981) J Bacteriol , vol.147 , pp. 1085-1094
    • Reichelt, B.Y.1    Fleet, G.H.2
  • 45
    • 0034220797 scopus 로고    scopus 로고
    • The primary structure of the subunit in Bacillus thermoamyloliquefaciens KP1071 molecular weight 540,000 homohexameric α-glucosidase II belonging to the glycosyl hydrolase family 31
    • S. Kashiwabara, S. Azuma, M. Tsuduki, and Y. Suzuki The primary structure of the subunit in Bacillus thermoamyloliquefaciens KP1071 molecular weight 540,000 homohexameric α-glucosidase II belonging to the glycosyl hydrolase family 31 Biosci Biotechnol Biochem 64 2000 1379 1393
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1379-1393
    • Kashiwabara, S.1    Azuma, S.2    Tsuduki, M.3    Suzuki, Y.4
  • 46
    • 0037474314 scopus 로고    scopus 로고
    • Change in maltose- and soluble starch-hydrolyzing activities of chimeric α-glucosidases of Mucor javanicus and Aspergillus oryzae
    • M. Sugimoto, T. Ohta, and F. Kawai Change in maltose- and soluble starch-hydrolyzing activities of chimeric α-glucosidases of Mucor javanicus and Aspergillus oryzae Biochim Biophys Acta 1645 2003 1 5
    • (2003) Biochim Biophys Acta , vol.1645 , pp. 1-5
    • Sugimoto, M.1    Ohta, T.2    Kawai, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.