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Volumn , Issue , 2016, Pages 2106-2118

A β-mannan utilization locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans

Author keywords

Bacteroides ovatus; galactomannan modification; GH36 galactosidase; polysaccharide utilization locus

Indexed keywords

ALPHA GALACTOSIDASE; BETA MANNAN; GH36 ALPHA GALACTOSIDASE; MANNAN; UNCLASSIFIED DRUG;

EID: 84979600169     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1002/1873-3468.12250     Document Type: Article
Times cited : (39)

References (41)
  • 2
    • 43849084710 scopus 로고    scopus 로고
    • How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation
    • Gilbert HJ, Stalbrand H and Brumer H (2008) How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation. Curr Opin Plant Biol 11, 338–348.
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 338-348
    • Gilbert, H.J.1    Stalbrand, H.2    Brumer, H.3
  • 3
    • 0034819282 scopus 로고    scopus 로고
    • Cloning and characterization of Aspergillus niger genes encoding an alpha-galactosidase and a beta-mannosidase involved in galactomannan degradation
    • Ademark P, de Vries RP, Hagglund P, Stalbrand H and Visser J (2001) Cloning and characterization of Aspergillus niger genes encoding an alpha-galactosidase and a beta-mannosidase involved in galactomannan degradation. Eur J Biochem 268, 2982–2990.
    • (2001) Eur J Biochem , vol.268 , pp. 2982-2990
    • Ademark, P.1    de Vries, R.P.2    Hagglund, P.3    Stalbrand, H.4    Visser, J.5
  • 4
    • 77956258531 scopus 로고    scopus 로고
    • Structural analysis of Saccharomyces cerevisiae alpha-galactosidase and its complexes with natural substrates reveals new insights into substrate specificity of GH27 glycosidases
    • Fernandez-Leiro R, Pereira-Rodriguez A, Cerdan ME, Becerra M and Sanz-Aparicio J (2010) Structural analysis of Saccharomyces cerevisiae alpha-galactosidase and its complexes with natural substrates reveals new insights into substrate specificity of GH27 glycosidases. J Biol Chem 285, 28020–28033.
    • (2010) J Biol Chem , vol.285 , pp. 28020-28033
    • Fernandez-Leiro, R.1    Pereira-Rodriguez, A.2    Cerdan, M.E.3    Becerra, M.4    Sanz-Aparicio, J.5
  • 5
    • 58849118994 scopus 로고    scopus 로고
    • Purification and characterization of thermostable alpha-galactosidase from Aspergillus terreus (GR)
    • Shankar SK, Dhananjay SK and Mulimani VH (2009) Purification and characterization of thermostable alpha-galactosidase from Aspergillus terreus (GR). Appl Biochem Biotechnol 152, 275–285.
    • (2009) Appl Biochem Biotechnol , vol.152 , pp. 275-285
    • Shankar, S.K.1    Dhananjay, S.K.2    Mulimani, V.H.3
  • 6
    • 0032103923 scopus 로고    scopus 로고
    • Thermostable alpha-galactosidase from Thermotoga neapolitana: cloning, sequencing and expression
    • King MR, Yernool DA, Eveleigh DE and Chassy BM (1998) Thermostable alpha-galactosidase from Thermotoga neapolitana: cloning, sequencing and expression. FEMS Microbiol Lett 163, 37–42.
    • (1998) FEMS Microbiol Lett , vol.163 , pp. 37-42
    • King, M.R.1    Yernool, D.A.2    Eveleigh, D.E.3    Chassy, B.M.4
  • 7
    • 33947433621 scopus 로고    scopus 로고
    • Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases
    • Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H and Kelly RM (2007) Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry 46, 3319–3330.
    • (2007) Biochemistry , vol.46 , pp. 3319-3330
    • Comfort, D.A.1    Bobrov, K.S.2    Ivanen, D.R.3    Shabalin, K.A.4    Harris, J.M.5    Kulminskaya, A.A.6    Brumer, H.7    Kelly, R.M.8
  • 9
    • 84855958136 scopus 로고    scopus 로고
    • Aga1, the first alpha-Galactosidase from the human bacteria Ruminococcus gnavus E1, efficiently transcribed in gut conditions
    • Aguilera M, Rakotoarivonina H, Brutus A, Giardina T, Simon G and Fons M (2012) Aga1, the first alpha-Galactosidase from the human bacteria Ruminococcus gnavus E1, efficiently transcribed in gut conditions. Res Microbiol 163, 14–21.
    • (2012) Res Microbiol , vol.163 , pp. 14-21
    • Aguilera, M.1    Rakotoarivonina, H.2    Brutus, A.3    Giardina, T.4    Simon, G.5    Fons, M.6
  • 10
    • 84873971576 scopus 로고    scopus 로고
    • The molecular mechanism of thermostable alpha-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies
    • Merceron R, Foucault M, Haser R, Mattes R, Watzlawick H and Gouet P (2012) The molecular mechanism of thermostable alpha-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies. J Biol Chem 287, 39642–39652.
    • (2012) J Biol Chem , vol.287 , pp. 39642-39652
    • Merceron, R.1    Foucault, M.2    Haser, R.3    Mattes, R.4    Watzlawick, H.5    Gouet, P.6
  • 11
    • 42649129680 scopus 로고    scopus 로고
    • An overview of mannan structure and mannan-degrading enzyme systems
    • Moreira LR and Filho EX (2008) An overview of mannan structure and mannan-degrading enzyme systems. Appl Microbiol Biotechnol 79, 165–178.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 165-178
    • Moreira, L.R.1    Filho, E.X.2
  • 12
    • 80052363804 scopus 로고    scopus 로고
    • Crystal structure of alpha-galactosidase from Lactobacillus acidophilus NCFM: insight into tetramer formation and substrate binding
    • Fredslund F, Hachem MA, Larsen RJ, Sorensen PG, Coutinho PM, Lo Leggio L and Svensson B (2011) Crystal structure of alpha-galactosidase from Lactobacillus acidophilus NCFM: insight into tetramer formation and substrate binding. J Mol Biol 412, 466–480.
    • (2011) J Mol Biol , vol.412 , pp. 466-480
    • Fredslund, F.1    Hachem, M.A.2    Larsen, R.J.3    Sorensen, P.G.4    Coutinho, P.M.5    Lo Leggio, L.6    Svensson, B.7
  • 14
    • 33750538870 scopus 로고    scopus 로고
    • A thermostable alpha-galactosidase from Lactobacillus fermentum CRL722: genetic characterization and main properties
    • Carrera-Silva EA, Silvestroni A, LeBlanc JG, Piard JC, Savoy de Giori G and Sesma F (2006) A thermostable alpha-galactosidase from Lactobacillus fermentum CRL722: genetic characterization and main properties. Curr Microbiol 53, 374–378.
    • (2006) Curr Microbiol , vol.53 , pp. 374-378
    • Carrera-Silva, E.A.1    Silvestroni, A.2    LeBlanc, J.G.3    Piard, J.C.4    Savoy de Giori, G.5    Sesma, F.6
  • 15
    • 84863734797 scopus 로고    scopus 로고
    • Development of a double-crossover markerless gene deletion system in Bifidobacterium longum: functional analysis of the alpha-galactosidase gene for raffinose assimilation
    • Hirayama Y, Sakanaka M, Fukuma H, Murayama H, Kano Y, Fukiya S and Yokota A (2012) Development of a double-crossover markerless gene deletion system in Bifidobacterium longum: functional analysis of the alpha-galactosidase gene for raffinose assimilation. Appl Environ Microbiol 78, 4984–4994.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 4984-4994
    • Hirayama, Y.1    Sakanaka, M.2    Fukuma, H.3    Murayama, H.4    Kano, Y.5    Fukiya, S.6    Yokota, A.7
  • 20
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G and Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8, 785–786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 22
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • Robert X and Gouet P (2014) Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res 42, W320–W324.
    • (2014) Nucleic Acids Res , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2
  • 23
    • 0037289902 scopus 로고    scopus 로고
    • Characterization of galactoglucomannan extracted from spruce (Picea abies) by heat-fractionation at different conditions
    • Lundqvist J, Jacobs A, Palm M, Zacchi G, Dahlman O and Stalbrand H (2003) Characterization of galactoglucomannan extracted from spruce (Picea abies) by heat-fractionation at different conditions. Carbohydr Polym 51, 203–211.
    • (2003) Carbohydr Polym , vol.51 , pp. 203-211
    • Lundqvist, J.1    Jacobs, A.2    Palm, M.3    Zacchi, G.4    Dahlman, O.5    Stalbrand, H.6
  • 26
    • 0025729215 scopus 로고
    • Subsite structure of Saccharomycopsis alpha-amylase secreted from Saccharomyces-Cerevisiae
    • Matsui I, Ishikawa K, Matsui E, Miyairi S, Fukui S and Honda K (1991) Subsite structure of Saccharomycopsis alpha-amylase secreted from Saccharomyces-Cerevisiae. J Biochem 109, 566–569.
    • (1991) J Biochem , vol.109 , pp. 566-569
    • Matsui, I.1    Ishikawa, K.2    Matsui, E.3    Miyairi, S.4    Fukui, S.5    Honda, K.6
  • 28
    • 84857914228 scopus 로고    scopus 로고
    • In situ enzymatic aided formation of xylan hydrogels and encapsulation of horse radish peroxidase for slow release
    • Chimphango AFA, van Zyl WH and Gorgens JF (2012) In situ enzymatic aided formation of xylan hydrogels and encapsulation of horse radish peroxidase for slow release. Carbohydr Polym 88, 1109–1117.
    • (2012) Carbohydr Polym , vol.88 , pp. 1109-1117
    • Chimphango, A.F.A.1    van Zyl, W.H.2    Gorgens, J.F.3
  • 29
    • 78649320840 scopus 로고    scopus 로고
    • A new alpha-galactosidase from symbiotic Flavobacterium sp. TN17 reveals four residues essential for alpha-galactosidase activity of gastrointestinal bacteria
    • Zhou J, Shi P, Huang H, Cao Y, Meng K, Yang P, Zhang R, Chen X and Yao B (2010) A new alpha-galactosidase from symbiotic Flavobacterium sp. TN17 reveals four residues essential for alpha-galactosidase activity of gastrointestinal bacteria. Appl Microbiol Biotechnol 88, 1297–1309.
    • (2010) Appl Microbiol Biotechnol , vol.88 , pp. 1297-1309
    • Zhou, J.1    Shi, P.2    Huang, H.3    Cao, Y.4    Meng, K.5    Yang, P.6    Zhang, R.7    Chen, X.8    Yao, B.9
  • 30
    • 84871273671 scopus 로고    scopus 로고
    • Metabolic mechanism of mannan in a ruminal bacterium, Ruminococcus albus, involving two mannoside phosphorylases and cellobiose 2-epimerase: discovery of a new carbohydrate phosphorylase, beta-1,4-mannooligosaccharide phosphorylase
    • Kawahara R, Saburi W, Odaka R, Taguchi H, Ito S, Mori H and Matsui H (2012) Metabolic mechanism of mannan in a ruminal bacterium, Ruminococcus albus, involving two mannoside phosphorylases and cellobiose 2-epimerase: discovery of a new carbohydrate phosphorylase, beta-1,4-mannooligosaccharide phosphorylase. J Biol Chem 287, 42389–42399.
    • (2012) J Biol Chem , vol.287 , pp. 42389-42399
    • Kawahara, R.1    Saburi, W.2    Odaka, R.3    Taguchi, H.4    Ito, S.5    Mori, H.6    Matsui, H.7
  • 31
  • 32
    • 0021919640 scopus 로고
    • Purification and characterization of two alpha-galactosidases associated with catabolism of guar gum and other alpha-galactosides by Bacteroides ovatus
    • Gherardini F, Babcock M and Salyers AA (1985) Purification and characterization of two alpha-galactosidases associated with catabolism of guar gum and other alpha-galactosides by Bacteroides ovatus. J Bacteriol 161, 500–506.
    • (1985) J Bacteriol , vol.161 , pp. 500-506
    • Gherardini, F.1    Babcock, M.2    Salyers, A.A.3
  • 33
    • 0026703920 scopus 로고
    • Analysis of proteins associated with growth of Bacteroides ovatus on the branched galactomannan guar gum
    • Valentine PJ and Salyers AA (1992) Analysis of proteins associated with growth of Bacteroides ovatus on the branched galactomannan guar gum. Appl Environ Microbiol 58, 1534–1540.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 1534-1540
    • Valentine, P.J.1    Salyers, A.A.2
  • 34
    • 84871881296 scopus 로고    scopus 로고
    • Expression and characterization of a Bifidobacterium adolescentis beta-mannanase carrying mannan-binding and cell association motifs
    • Kulcinskaja E, Rosengren A, Ibrahim R, Kolenova K and Stalbrand H (2013) Expression and characterization of a Bifidobacterium adolescentis beta-mannanase carrying mannan-binding and cell association motifs. Appl Environ Microbiol 79, 133–140.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 133-140
    • Kulcinskaja, E.1    Rosengren, A.2    Ibrahim, R.3    Kolenova, K.4    Stalbrand, H.5
  • 35
    • 84947866821 scopus 로고    scopus 로고
    • The GH5 1,4-beta-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes
    • Morrill J, Kulcinskaja E, Sulewska AM, Lahtinen S, Stalbrand H, Svensson B and Abou Hachem M (2015) The GH5 1,4-beta-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes. BMC Biochem 16, 26.
    • (2015) BMC Biochem , vol.16 , pp. 26
    • Morrill, J.1    Kulcinskaja, E.2    Sulewska, A.M.3    Lahtinen, S.4    Stalbrand, H.5    Svensson, B.6    Abou Hachem, M.7
  • 37
    • 0025825772 scopus 로고
    • A Bacteroides ovatus chromosomal locus which contains an alpha-galactosidase gene may be important for colonization of the gastrointestinal tract
    • Valentine PJ, Gherardini FC and Salyers AA (1991) A Bacteroides ovatus chromosomal locus which contains an alpha-galactosidase gene may be important for colonization of the gastrointestinal tract. Appl Environ Microbiol 57, 1615–1623.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 1615-1623
    • Valentine, P.J.1    Gherardini, F.C.2    Salyers, A.A.3
  • 38
    • 84933679807 scopus 로고    scopus 로고
    • A review of the enzymatic hydrolysis of mannans and synergistic interactions between beta-mannanase, beta-mannosidase and alpha-galactosidase
    • Malgas S, van Dyk JS and Pletschke BI (2015) A review of the enzymatic hydrolysis of mannans and synergistic interactions between beta-mannanase, beta-mannosidase and alpha-galactosidase. World J Microbiol Biotechnol 31, 1167–1175.
    • (2015) World J Microbiol Biotechnol , vol.31 , pp. 1167-1175
    • Malgas, S.1    van Dyk, J.S.2    Pletschke, B.I.3
  • 39
    • 0023243835 scopus 로고
    • Purification and characterization of a cell-associated, soluble mannanase from Bacteroides ovatus
    • Gherardini FC and Salyers AA (1987) Purification and characterization of a cell-associated, soluble mannanase from Bacteroides ovatus. J Bacteriol 169, 2038–2043.
    • (1987) J Bacteriol , vol.169 , pp. 2038-2043
    • Gherardini, F.C.1    Salyers, A.A.2
  • 40
    • 0023184153 scopus 로고
    • Characterization of an outer membrane mannanase from Bacteroides ovatus
    • Gherardini FC and Salyers AA (1987) Characterization of an outer membrane mannanase from Bacteroides ovatus. J Bacteriol 169, 2031–2037.
    • (1987) J Bacteriol , vol.169 , pp. 2031-2037
    • Gherardini, F.C.1    Salyers, A.A.2


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