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Volumn 376, Issue 1, 2008, Pages 210-220

Crystal Structure of Aspergillus niger Isopullulanase, a Member of Glycoside Hydrolase Family 49

Author keywords

dextranase; GH49; isopullulanase; pullulan; helix

Indexed keywords

AMINO ACID; DEXTRAN; DEXTRANASE; FUNGAL ENZYME; GLUCOSE; GLYCOSIDASE; HELIX LOOP HELIX PROTEIN; ISOMALTOSE; ISOPANOSE; ISOPULLULANASE; N ACETYL BETA GLUCOSAMINIDASE; N ACETYLGLUCOSAMINE; OLIGOSACCHARIDE; POLYGALACTURONASE; POLYSACCHARIDE; PULLULAN; UNCLASSIFIED DRUG;

EID: 38049040779     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.098     Document Type: Article
Times cited : (23)

References (42)
  • 1
    • 33745466322 scopus 로고
    • Pullulan, an extracellular glucan from Pullularia pullulans
    • Bender H., Lehmann J., and Wallenfels K. Pullulan, an extracellular glucan from Pullularia pullulans. Biochim. Biophys. Acta 36 (1959) 309-316
    • (1959) Biochim. Biophys. Acta , vol.36 , pp. 309-316
    • Bender, H.1    Lehmann, J.2    Wallenfels, K.3
  • 2
    • 0842287586 scopus 로고    scopus 로고
    • Current knowledge on biosynthesis, biological activity, and chemical modification of the exopolysaccharide, pullulan
    • Shingel K.I. Current knowledge on biosynthesis, biological activity, and chemical modification of the exopolysaccharide, pullulan. Carbohydr. Res. 339 (2004) 447-460
    • (2004) Carbohydr. Res. , vol.339 , pp. 447-460
    • Shingel, K.I.1
  • 3
    • 0029089389 scopus 로고
    • Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47
    • Tonozuka T., Mogi S., Shimura Y., Ibuka A., Sakai H., Matsuzawa H., et al. Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47. Biochim. Biophys. Acta 1252 (1995) 35-42
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 35-42
    • Tonozuka, T.1    Mogi, S.2    Shimura, Y.3    Ibuka, A.4    Sakai, H.5    Matsuzawa, H.6
  • 5
    • 0032976301 scopus 로고    scopus 로고
    • The concept of the α-amylase family: structural similarity and common catalytic mechanism
    • Kuriki T., and Imanaka T. The concept of the α-amylase family: structural similarity and common catalytic mechanism. J. Biosci. Bioeng. 87 (1999) 557-565
    • (1999) J. Biosci. Bioeng. , vol.87 , pp. 557-565
    • Kuriki, T.1    Imanaka, T.2
  • 6
  • 7
    • 0030999008 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of the isopullulanase gene from Aspergillus niger ATCC 9642
    • Aoki H., Yopi, and Sakano Y. Molecular cloning and heterologous expression of the isopullulanase gene from Aspergillus niger ATCC 9642. Biochem. J. 323 (1997) 757-764
    • (1997) Biochem. J. , vol.323 , pp. 757-764
    • Aoki, H.1    Yopi2    Sakano, Y.3
  • 8
    • 0030908595 scopus 로고    scopus 로고
    • A classification of dextran-hydrolysing enzymes based on amino-acid-sequence similarities
    • Aoki H., and Sakano Y. A classification of dextran-hydrolysing enzymes based on amino-acid-sequence similarities. Biochem. J. 323 (1997) 859-861
    • (1997) Biochem. J. , vol.323 , pp. 859-861
    • Aoki, H.1    Sakano, Y.2
  • 9
    • 9644279704 scopus 로고    scopus 로고
    • Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase
    • Akeboshi H., Tonozuka T., Furukawa T., Ichikawa K., Aoki H., Shimonishi A., et al. Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase. Eur. J. Biochem. 271 (2004) 4420-4427
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4420-4427
    • Akeboshi, H.1    Tonozuka, T.2    Furukawa, T.3    Ichikawa, K.4    Aoki, H.5    Shimonishi, A.6
  • 10
    • 0033256386 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the gene for glucodextranase from Arthrobacter globiformis T-3044 and expression in Escherichia coli cells
    • Oguma T., Kurokawa T., Tobe K., Kitao S., and Kobayashi M. Cloning and sequence analysis of the gene for glucodextranase from Arthrobacter globiformis T-3044 and expression in Escherichia coli cells. Biosci. Biotechnol. Biochem. 63 (1999) 2174-2182
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 2174-2182
    • Oguma, T.1    Kurokawa, T.2    Tobe, K.3    Kitao, S.4    Kobayashi, M.5
  • 11
    • 0025869966 scopus 로고
    • Molecular cloning and nucleotide sequencing of the Arthrobacter dextranase gene and its expression in Escherichia coli and Streptococcus sanguis
    • Okushima M., Sugino D., Kouno Y., Nakano S., Miyahara J., Toda H., et al. Molecular cloning and nucleotide sequencing of the Arthrobacter dextranase gene and its expression in Escherichia coli and Streptococcus sanguis. Jpn. J. Genet. 66 (1991) 173-187
    • (1991) Jpn. J. Genet. , vol.66 , pp. 173-187
    • Okushima, M.1    Sugino, D.2    Kouno, Y.3    Nakano, S.4    Miyahara, J.5    Toda, H.6
  • 12
    • 0029790702 scopus 로고    scopus 로고
    • Cloning of the Penicillium minioluteum gene encoding dextranase and its expression in Pichia pastoris
    • Roca H., Garcia B., Rodriguez E., Mateu D., Coroas L., Cremata J., et al. Cloning of the Penicillium minioluteum gene encoding dextranase and its expression in Pichia pastoris. Yeast 12 (1996) 1187-1200
    • (1996) Yeast , vol.12 , pp. 1187-1200
    • Roca, H.1    Garcia, B.2    Rodriguez, E.3    Mateu, D.4    Coroas, L.5    Cremata, J.6
  • 13
    • 0042334876 scopus 로고    scopus 로고
    • Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex
    • Larsson A.M., Andersson R., Stahlberg J., Kenne L., and Jones T.A. Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex. Structure 11 (2003) 1111-1121
    • (2003) Structure , vol.11 , pp. 1111-1121
    • Larsson, A.M.1    Andersson, R.2    Stahlberg, J.3    Kenne, L.4    Jones, T.A.5
  • 14
    • 0033195840 scopus 로고    scopus 로고
    • Molecular cloning of isomaltotrio-dextranase gene from Brevibacterium fuscum var. dextranlyticum strain 0407 and its expression in Escherichia coli
    • Mizuno T., Mori H., Ito H., Matsui H., Kimura A., and Chiba S. Molecular cloning of isomaltotrio-dextranase gene from Brevibacterium fuscum var. dextranlyticum strain 0407 and its expression in Escherichia coli. Biosci. Biotechnol. Biochem. 63 (1999) 1582-1588
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1582-1588
    • Mizuno, T.1    Mori, H.2    Ito, H.3    Matsui, H.4    Kimura, A.5    Chiba, S.6
  • 15
    • 0027329090 scopus 로고
    • New domain motif: the structure of pectate lyase C, a secreted plant virulence factor
    • Yoder M.D., Keen N.T., and Jurnak F. New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260 (1993) 1503-1507
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 16
    • 0035955653 scopus 로고    scopus 로고
    • The ι-carrageenase of Alteromonas fortis. A β-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide
    • Michel G., Chantalat L., Fanchon E., Henrissat B., Kloareg B., and Dideberg O. The ι-carrageenase of Alteromonas fortis. A β-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide. J. Biol. Chem. 276 (2001) 40202-40209
    • (2001) J. Biol. Chem. , vol.276 , pp. 40202-40209
    • Michel, G.1    Chantalat, L.2    Fanchon, E.3    Henrissat, B.4    Kloareg, B.5    Dideberg, O.6
  • 18
    • 0031688287 scopus 로고    scopus 로고
    • Structure and evolution of parallel β-helix proteins
    • Jenkins J., Mayans O., and Pickersgill R. Structure and evolution of parallel β-helix proteins. J. Struct. Biol. 122 (1998) 236-246
    • (1998) J. Struct. Biol. , vol.122 , pp. 236-246
    • Jenkins, J.1    Mayans, O.2    Pickersgill, R.3
  • 19
    • 0030293906 scopus 로고    scopus 로고
    • Two components of cell-bound isopullulanase from Aspergillus niger ATCC 9642-their purification and enzymatic properties
    • Aoki H., Yopi, Padmajanti A., and Sakano Y. Two components of cell-bound isopullulanase from Aspergillus niger ATCC 9642-their purification and enzymatic properties. Biosci. Biotech. Biochem. 60 (1996) 1795-1798
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 1795-1798
    • Aoki, H.1    Yopi2    Padmajanti, A.3    Sakano, Y.4
  • 20
    • 1542649848 scopus 로고    scopus 로고
    • Construction of an efficient expression system for Aspergillus isopullulanase in Pichia pastoris, and a simple purification method
    • Akeboshi H., Kashiwagi Y., Aoki H., Tonozuka T., Atsushi N., and Sakano Y. Construction of an efficient expression system for Aspergillus isopullulanase in Pichia pastoris, and a simple purification method. Biosci. Biotechnol. Biochem. 67 (2003) 1149-1153
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1149-1153
    • Akeboshi, H.1    Kashiwagi, Y.2    Aoki, H.3    Tonozuka, T.4    Atsushi, N.5    Sakano, Y.6
  • 21
    • 4544294812 scopus 로고    scopus 로고
    • Deglycosylated isopullulanase retains enzymatic activity
    • Padmajanti A., Tonozuka T., and Sakano Y. Deglycosylated isopullulanase retains enzymatic activity. J. Appl. Glycosci. 47 (2000) 287-292
    • (2000) J. Appl. Glycosci. , vol.47 , pp. 287-292
    • Padmajanti, A.1    Tonozuka, T.2    Sakano, Y.3
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. A program for photorealistic molecular graphics
    • Merritt E.A., and Murphy M.E.P. Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. Sect. D 50 (1994) 869-873
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 24
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 25
    • 33846113064 scopus 로고    scopus 로고
    • Recent structural studies of carbohydrate-binding modules
    • Hashimoto H. Recent structural studies of carbohydrate-binding modules. Cell. Mol. Life Sci. 63 (2006) 2954-2967
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2954-2967
    • Hashimoto, H.1
  • 26
    • 0037188358 scopus 로고    scopus 로고
    • Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution
    • Shimizu T., Nakatsu T., Miyairi K., Okuno T., and Kato H. Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution. Biochemistry 41 (2002) 6651-6659
    • (2002) Biochemistry , vol.41 , pp. 6651-6659
    • Shimizu, T.1    Nakatsu, T.2    Miyairi, K.3    Okuno, T.4    Kato, H.5
  • 27
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies G.J., Wilson K.S., and Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321 (1997) 557-559
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 28
    • 0032714568 scopus 로고    scopus 로고
    • Importance of glycosidases in mammalian glycoprotein biosynthesis
    • Herscovics A. Importance of glycosidases in mammalian glycoprotein biosynthesis. Biochim. Biophys. Acta 1473 (1999) 96-107
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 96-107
    • Herscovics, A.1
  • 29
    • 0017869154 scopus 로고
    • Endo-β-N-acetylglucosaminidase from Streptomyces plicatus
    • Tarentino A.L., Trimble R.B., and Maley F. Endo-β-N-acetylglucosaminidase from Streptomyces plicatus. Methods Enzymol. 50 (1978) 574-580
    • (1978) Methods Enzymol. , vol.50 , pp. 574-580
    • Tarentino, A.L.1    Trimble, R.B.2    Maley, F.3
  • 30
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., and Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8 (1995) 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 31
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 32
    • 0032544357 scopus 로고    scopus 로고
    • Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora
    • Pickersgill R., Smith D., Worboys K., and Jenkins J. Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora. J. Biol. Chem. 273 (1998) 24660-24664
    • (1998) J. Biol. Chem. , vol.273 , pp. 24660-24664
    • Pickersgill, R.1    Smith, D.2    Worboys, K.3    Jenkins, J.4
  • 33
    • 0032589464 scopus 로고    scopus 로고
    • 1.68-Å crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis
    • van Santen Y., Benen J.A., Schroter K.H., Kalk K.H., Armand S., Visser J., and Dijkstra B.W. 1.68-Å crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis. J. Biol. Chem. 274 (1999) 30474-30480
    • (1999) J. Biol. Chem. , vol.274 , pp. 30474-30480
    • van Santen, Y.1    Benen, J.A.2    Schroter, K.H.3    Kalk, K.H.4    Armand, S.5    Visser, J.6    Dijkstra, B.W.7
  • 34
    • 0035823490 scopus 로고    scopus 로고
    • Changing a single amino acid residue switches processive and non-processive behavior of Aspergillus niger endopolygalacturonase I and II
    • Pagès S., Kester H.C., Visser J., and Benen J.A. Changing a single amino acid residue switches processive and non-processive behavior of Aspergillus niger endopolygalacturonase I and II. J. Biol. Chem. 276 (2001) 33652-33656
    • (2001) J. Biol. Chem. , vol.276 , pp. 33652-33656
    • Pagès, S.1    Kester, H.C.2    Visser, J.3    Benen, J.A.4
  • 35
    • 0242457394 scopus 로고    scopus 로고
    • Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger
    • van Pouderoyen G., Snijder H.J., Benen J.A., and Dijkstra B.W. Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger. FEBS Lett. 554 (2003) 462-466
    • (2003) FEBS Lett. , vol.554 , pp. 462-466
    • van Pouderoyen, G.1    Snijder, H.J.2    Benen, J.A.3    Dijkstra, B.W.4
  • 36
    • 0035943418 scopus 로고    scopus 로고
    • The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex
    • Cho S.W., Lee S., and Shin W. The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex. J. Mol. Biol. 11 (2001) 863-878
    • (2001) J. Mol. Biol. , vol.11 , pp. 863-878
    • Cho, S.W.1    Lee, S.2    Shin, W.3
  • 37
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 0002705842 scopus 로고
    • XtalView: a visual protein crystallographic software system for XII/XView
    • McRee D. XtalView: a visual protein crystallographic software system for XII/XView. J. Mol. Graphics 10 (1992) 44-47
    • (1992) J. Mol. Graphics , vol.10 , pp. 44-47
    • McRee, D.1
  • 42
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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