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Volumn 51, Issue 6-7, 2012, Pages 359-365

Crystal structure of a lactosucrose-producing enzyme, Arthrobacter sp. K-1 β-fructofuranosidase

Author keywords

Fructofuranosidase; Propeller; ArFFase; BsLev; GdLev; GH; Glycoside hydrolase family 68; Lactosucrose; Levansucrase

Indexed keywords

ARFFASE; BSLEV; GDLEV; GH; GLYCOSIDE HYDROLASES; LACTOSUCROSE; LEVANSUCRASE;

EID: 84867204725     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2012.08.004     Document Type: Article
Times cited : (35)

References (52)
  • 5
    • 21144440174 scopus 로고
    • Enzymatic synthesis and characterization of a new trisaccharide, α-lactosyl-β-fructofuranoside
    • Avigad G. Enzymatic synthesis and characterization of a new trisaccharide, α-lactosyl-β-fructofuranoside. Journal of Biological Chemistry 1957, 229:121-129.
    • (1957) Journal of Biological Chemistry , vol.229 , pp. 121-129
    • Avigad, G.1
  • 13
    • 0242490546 scopus 로고    scopus 로고
    • Structural framework of fructosyl transfer in Bacillus subtilis levansucrase
    • Meng G., Fütterer K. Structural framework of fructosyl transfer in Bacillus subtilis levansucrase. Nature Structural Biology 2003, 10:935-941.
    • (2003) Nature Structural Biology , vol.10 , pp. 935-941
    • Meng, G.1    Fütterer, K.2
  • 14
    • 41549120638 scopus 로고    scopus 로고
    • Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase Bacillus subtilis levansucrase
    • Meng G., Fütterer K. Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase Bacillus subtilis levansucrase. BMC Structural Biology 2008, 8:16.
    • (2008) BMC Structural Biology , vol.8 , pp. 16
    • Meng, G.1    Fütterer, K.2
  • 15
    • 79955961857 scopus 로고    scopus 로고
    • Polysaccharide synthesis of the levansucrase SacB from Bacillus megaterium is controlled by distinct surface motifs
    • Strube C.P., Homann A., Gamer M., Jahn D., Seibel J., Heinz D.W. Polysaccharide synthesis of the levansucrase SacB from Bacillus megaterium is controlled by distinct surface motifs. Journal of Biological Chemistry 2011, 286:17593-17600.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 17593-17600
    • Strube, C.P.1    Homann, A.2    Gamer, M.3    Jahn, D.4    Seibel, J.5    Heinz, D.W.6
  • 17
    • 84860389478 scopus 로고    scopus 로고
    • Crystal structure of inulosucrase from Lactobacillus: insights into the substrate specificity and product specificity of GH68 fructansucrases
    • Pijning T., Anwar M.A., Böger M., Dobruchowska J.M., Leemhuis H., Kralj S., et al. Crystal structure of inulosucrase from Lactobacillus: insights into the substrate specificity and product specificity of GH68 fructansucrases. Journal of Molecular Biology 2011, 412:80-93.
    • (2011) Journal of Molecular Biology , vol.412 , pp. 80-93
    • Pijning, T.1    Anwar, M.A.2    Böger, M.3    Dobruchowska, J.M.4    Leemhuis, H.5    Kralj, S.6
  • 18
    • 33846541543 scopus 로고    scopus 로고
    • Hyperproduction and application of alpha-agarase to enzymatic enhancement of antioxidant of porphyran
    • Hatada Y., Ohta Y., Horikoshi K. Hyperproduction and application of alpha-agarase to enzymatic enhancement of antioxidant of porphyran. Journal of Agricultural and Food Chemistry 2006, 54:9895-9900.
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , pp. 9895-9900
    • Hatada, Y.1    Ohta, Y.2    Horikoshi, K.3
  • 19
    • 29244437175 scopus 로고    scopus 로고
    • Sequence of the gene for a high-alkaline mannanase from an alkaliphilic Bacillus sp. strain JAMB-750, its expression in Bacillus subtilis and characterization of the recombinant enzyme
    • Hatada Y., Takeda N., Hirasawa K., Ohta Y., Usami R., Yoshida Y., et al. Sequence of the gene for a high-alkaline mannanase from an alkaliphilic Bacillus sp. strain JAMB-750, its expression in Bacillus subtilis and characterization of the recombinant enzyme. Extremophiles 2005, 9:497-500.
    • (2005) Extremophiles , vol.9 , pp. 497-500
    • Hatada, Y.1    Takeda, N.2    Hirasawa, K.3    Ohta, Y.4    Usami, R.5    Yoshida, Y.6
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology 1997, 276:307-326.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project The CCP4 suite: programs for protein crystallography. Acta Crystallographica. Section D: Biological Crystallography 1994, 50:760-763.
    • (1994) Acta Crystallographica. Section D: Biological Crystallography , vol.50 , pp. 760-763
  • 22
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nature Structural Biology 1999, 6:458-463.
    • (1999) Nature Structural Biology , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 24
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Engineering 1995, 8:127-134.
    • (1995) Protein Engineering , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 26
    • 1042291218 scopus 로고    scopus 로고
    • Three acidic residues are at the active site of a beta-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68
    • Pons T., Naumoff D.G., Martínez-Fleites C., Hernández L. Three acidic residues are at the active site of a beta-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68. Proteins 2004, 54:424-432.
    • (2004) Proteins , vol.54 , pp. 424-432
    • Pons, T.1    Naumoff, D.G.2    Martínez-Fleites, C.3    Hernández, L.4
  • 27
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. Journal of Molecular Biology 1993, 233:123-138.
    • (1993) Journal of Molecular Biology , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 29
    • 33646165074 scopus 로고    scopus 로고
    • The structure of an inverting GH43 β-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role of the three catalytic residues
    • Brux C., Ben-David A., Shallom-Shezifi D., Leon M., Niefind K., Shoham G., et al. The structure of an inverting GH43 β-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role of the three catalytic residues. Journal of Molecular Biology 2006, 359:97-109.
    • (2006) Journal of Molecular Biology , vol.359 , pp. 97-109
    • Brux, C.1    Ben-David, A.2    Shallom-Shezifi, D.3    Leon, M.4    Niefind, K.5    Shoham, G.6
  • 30
    • 33646253657 scopus 로고    scopus 로고
    • Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose
    • Alberto F., Jordi E., Henrissat B., Czjzek M. Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose. Biochemical Journal 2006, 395:457-462.
    • (2006) Biochemical Journal , vol.395 , pp. 457-462
    • Alberto, F.1    Jordi, E.2    Henrissat, B.3    Czjzek, M.4
  • 31
    • 79955588033 scopus 로고    scopus 로고
    • Crystal structures of the apo form of β-fructofuranosidase from Bifidobacterium longum and its complex with fructose
    • Bujacz A., Jedrzejczak-Krzepkowska M., Bielecki S., Redzynia I., Bujacz G. Crystal structures of the apo form of β-fructofuranosidase from Bifidobacterium longum and its complex with fructose. FEBS Journal 2011, 278:1728-1744.
    • (2011) FEBS Journal , vol.278 , pp. 1728-1744
    • Bujacz, A.1    Jedrzejczak-Krzepkowska, M.2    Bielecki, S.3    Redzynia, I.4    Bujacz, G.5
  • 32
    • 84862618287 scopus 로고    scopus 로고
    • Furanosidase superfamily: search of homologues
    • Naumoff D.G. Furanosidase superfamily: search of homologues. Molecular Biology 2012, 46:354-360.
    • (2012) Molecular Biology , vol.46 , pp. 354-360
    • Naumoff, D.G.1
  • 33
    • 0037006986 scopus 로고    scopus 로고
    • High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding
    • Notenboom V., Boraston A.B., Williams S.J., Kilburn D.G., Rose D.R. High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding. Biochemistry 2002, 41:4246-4254.
    • (2002) Biochemistry , vol.41 , pp. 4246-4254
    • Notenboom, V.1    Boraston, A.B.2    Williams, S.J.3    Kilburn, D.G.4    Rose, D.R.5
  • 34
    • 16244415566 scopus 로고    scopus 로고
    • Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability
    • Chen Y., Delmas J., Sirot J., Shoichet B., Bonnet R. Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability. Journal of Molecular Biology 2005, 348:349-362.
    • (2005) Journal of Molecular Biology , vol.348 , pp. 349-362
    • Chen, Y.1    Delmas, J.2    Sirot, J.3    Shoichet, B.4    Bonnet, R.5
  • 35
    • 77954925220 scopus 로고    scopus 로고
    • Crystal structures of Aspergillus japonicus fructosyltransferase complex with donor/acceptor substrates reveal complete subsites in the active site for catalysis
    • Chuankhayan P., Hsieh C.Y., Huang Y.C., Hsieh Y.Y., Guan H.H., Hsieh Y.C., et al. Crystal structures of Aspergillus japonicus fructosyltransferase complex with donor/acceptor substrates reveal complete subsites in the active site for catalysis. Journal of Biological Chemistry 2010, 285:23251-23264.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 23251-23264
    • Chuankhayan, P.1    Hsieh, C.Y.2    Huang, Y.C.3    Hsieh, Y.Y.4    Guan, H.H.5    Hsieh, Y.C.6
  • 36
    • 0025861055 scopus 로고
    • Polymerase and hydrolase activities of Bacillus subtilis levansucrase can be separately modulated by site-directed mutagenesis
    • Chambert R., Petit-Glatron M.F. Polymerase and hydrolase activities of Bacillus subtilis levansucrase can be separately modulated by site-directed mutagenesis. Biochemical Journal 1991, 279:35-41.
    • (1991) Biochemical Journal , vol.279 , pp. 35-41
    • Chambert, R.1    Petit-Glatron, M.F.2
  • 37
    • 0036775911 scopus 로고    scopus 로고
    • Identification of functionally important amino acid residues in Zymomonas mobilis levansucrase
    • Yanase H., Maeda M., Hagiwara E., Yagi H., Taniguchi K., Okamoto K. Identification of functionally important amino acid residues in Zymomonas mobilis levansucrase. Journal of Biochemistry 2002, 132:565-572.
    • (2002) Journal of Biochemistry , vol.132 , pp. 565-572
    • Yanase, H.1    Maeda, M.2    Hagiwara, E.3    Yagi, H.4    Taniguchi, K.5    Okamoto, K.6
  • 38
    • 41549112339 scopus 로고    scopus 로고
    • Amino acid substitutions of His296 alter the catalytic properties of Zymomonas mobilis 10232 levansucrase
    • Li S.Y., Chen M., Li G., Yan Y.L., Yu H.Y., Zhan Y.H., et al. Amino acid substitutions of His296 alter the catalytic properties of Zymomonas mobilis 10232 levansucrase. Acta Biochimica Polonica 2008, 55:201-206.
    • (2008) Acta Biochimica Polonica , vol.55 , pp. 201-206
    • Li, S.Y.1    Chen, M.2    Li, G.3    Yan, Y.L.4    Yu, H.Y.5    Zhan, Y.H.6
  • 40
    • 35048826148 scopus 로고    scopus 로고
    • Insights into polymer versus oligosaccharide synthesis: mutagenesis and mechanistic studies of a novel levansucrase from Bacillus megaterium
    • Homann A., Biedendieck R., Götze S., Jahn D., Seibel J. Insights into polymer versus oligosaccharide synthesis: mutagenesis and mechanistic studies of a novel levansucrase from Bacillus megaterium. Biochemical Journal 2007, 407:189-198.
    • (2007) Biochemical Journal , vol.407 , pp. 189-198
    • Homann, A.1    Biedendieck, R.2    Götze, S.3    Jahn, D.4    Seibel, J.5
  • 41
    • 84861407812 scopus 로고    scopus 로고
    • Computation of tunnels in protein molecules using Delaunay triangulation
    • Medek P., BeneŠ P., Sochor J. Computation of tunnels in protein molecules using Delaunay triangulation. Journal of WSCG 2007, 15:107-114.
    • (2007) Journal of WSCG , vol.15 , pp. 107-114
    • Medek, P.1    BeneŠ, P.2    Sochor, J.3
  • 43
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia C. Structural invariants in protein folding. Nature 1975, 254:304-308.
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 44
    • 41949139216 scopus 로고    scopus 로고
    • Substrate recognition mechanism of α-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans
    • Hondoh H., Saburi W., Mori H., Okuyama M., Nakada T., Matsuura Y., et al. Substrate recognition mechanism of α-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans. Journal of Molecular Biology 2008, 378:913-922.
    • (2008) Journal of Molecular Biology , vol.378 , pp. 913-922
    • Hondoh, H.1    Saburi, W.2    Mori, H.3    Okuyama, M.4    Nakada, T.5    Matsuura, Y.6
  • 45
    • 77957259893 scopus 로고    scopus 로고
    • Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose
    • Yamamoto K., Miyake H., Kusunoki M., Osaki S. Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose. FEBS Journal 2010, 277:4205-4214.
    • (2010) FEBS Journal , vol.277 , pp. 4205-4214
    • Yamamoto, K.1    Miyake, H.2    Kusunoki, M.3    Osaki, S.4
  • 46
    • 0032562777 scopus 로고    scopus 로고
    • Molecular structure of a barley α-amylase-inhibitor complex: implications for starch binding and catalysis
    • Kadziola A., Søgaard M., Svensson B., Haser R. Molecular structure of a barley α-amylase-inhibitor complex: implications for starch binding and catalysis. Journal of Molecular Biology 1998, 278:205-217.
    • (1998) Journal of Molecular Biology , vol.278 , pp. 205-217
    • Kadziola, A.1    Søgaard, M.2    Svensson, B.3    Haser, R.4
  • 47
    • 0037007004 scopus 로고    scopus 로고
    • Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic α-amylase
    • Aghajari N., Roth M., Haser R. Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic α-amylase. Biochemistry 2002, 41:4273-4280.
    • (2002) Biochemistry , vol.41 , pp. 4273-4280
    • Aghajari, N.1    Roth, M.2    Haser, R.3
  • 48
    • 10044276926 scopus 로고    scopus 로고
    • Lactosucrose bioconversion from lactose and sucrose by whole cells of Paenibacillus polymyxa harboring levansucrase activity
    • Choi H.J., Kim C.S., Kim P., Jung H.C., Oh D.K. Lactosucrose bioconversion from lactose and sucrose by whole cells of Paenibacillus polymyxa harboring levansucrase activity. Biotechnology Progress 2004, 20:1876-1879.
    • (2004) Biotechnology Progress , vol.20 , pp. 1876-1879
    • Choi, H.J.1    Kim, C.S.2    Kim, P.3    Jung, H.C.4    Oh, D.K.5
  • 49
    • 21144451878 scopus 로고    scopus 로고
    • Lactosucrose production by various microorganisms harboring levansucrase activity
    • Park N.H., Choi H.J., Oh D.K. Lactosucrose production by various microorganisms harboring levansucrase activity. Biotechnology Letters 2005, 27:495-497.
    • (2005) Biotechnology Letters , vol.27 , pp. 495-497
    • Park, N.H.1    Choi, H.J.2    Oh, D.K.3
  • 52
    • 0029034720 scopus 로고
    • Isolation and enzymic properties of levansucrase secreted by Acetobacter diazotrophicus SRT4, a bacterium associated with sugar cane
    • Hernandez L., Arrieta J., Menendez C., Vazquez R., Coego A., Suarez V., et al. Isolation and enzymic properties of levansucrase secreted by Acetobacter diazotrophicus SRT4, a bacterium associated with sugar cane. Biochemical Journal 1995, 309:113-118.
    • (1995) Biochemical Journal , vol.309 , pp. 113-118
    • Hernandez, L.1    Arrieta, J.2    Menendez, C.3    Vazquez, R.4    Coego, A.5    Suarez, V.6


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