메뉴 건너뛰기




Volumn 584, Issue 21, 2010, Pages 4435-4441

Consolidation of glycosyl hydrolase family 30: A dual domain 4/7 hydrolase family consisting of two structurally distinct groups

Author keywords

Endo 1,6 galactanase; Endo 1,6 glucanase; Glucosylceramidase; Glucuronoxylan xylanohydrolase; Glycosyl hydrolase family 30 (GH30); Glycosyl hydrolase family 5 (GH5)

Indexed keywords

AMINO ACID; GLYCOSIDASE;

EID: 78049264854     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.09.051     Document Type: Article
Times cited : (111)

References (51)
  • 1
    • 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. 1991, 280:309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 2
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. USA 1995, 92:7090-7094.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 4
    • 33845383205 scopus 로고    scopus 로고
    • Characterization of XynC from Bacillus subtilis subsp. subtilis strain 168 and analysis of its role in depolymerization of glucuronoxylan
    • St John F.J., Rice J.D., Preston J.F. Characterization of XynC from Bacillus subtilis subsp. subtilis strain 168 and analysis of its role in depolymerization of glucuronoxylan. J. Bacteriol. 2006, 188:8617-8626.
    • (2006) J. Bacteriol. , vol.188 , pp. 8617-8626
    • St John, F.J.1    Rice, J.D.2    Preston, J.F.3
  • 5
    • 33947201140 scopus 로고    scopus 로고
    • Mode of action of glycoside hydrolase family 5 glucuronoxylan xylanohydrolase from Erwinia chrysanthemi
    • Vrsanska M., Kolenova K., Puchart V., Biely P. Mode of action of glycoside hydrolase family 5 glucuronoxylan xylanohydrolase from Erwinia chrysanthemi. FEBS J. 2007, 274:1666-1677.
    • (2007) FEBS J. , vol.274 , pp. 1666-1677
    • Vrsanska, M.1    Kolenova, K.2    Puchart, V.3    Biely, P.4
  • 8
    • 33144487406 scopus 로고    scopus 로고
    • Microbial strategies for the depolymerization of glucuronoxylan: leads to biotechnological applications of endoxylanases
    • American Chemical Society, Washington DC
    • Preston J.F., Hurlbert J.C., Rice J.D., Ragunathan A., St.John F.J. Microbial strategies for the depolymerization of glucuronoxylan: leads to biotechnological applications of endoxylanases. Applications of Enzymes to Lignocellulosics 2003, vol. 855:191-210. American Chemical Society, Washington DC.
    • (2003) Applications of Enzymes to Lignocellulosics , vol.855 , pp. 191-210
    • Preston, J.F.1    Hurlbert, J.C.2    Rice, J.D.3    Ragunathan, A.4    St.John, F.J.5
  • 9
    • 33845490892 scopus 로고    scopus 로고
    • Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease
    • Brumshtein B., Wormald M.R., Silman I., Futerman A.H., Sussman J.L. Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease. Acta Crystallogr. D 2006, 62:1458-1465.
    • (2006) Acta Crystallogr. D , vol.62 , pp. 1458-1465
    • Brumshtein, B.1    Wormald, M.R.2    Silman, I.3    Futerman, A.H.4    Sussman, J.L.5
  • 10
    • 64949116944 scopus 로고    scopus 로고
    • Characterization of a putative endoxylanase in the migratory plant-parasitic nematode Radopholus similis
    • Haegeman A., Vanholme B., Gheysen G. Characterization of a putative endoxylanase in the migratory plant-parasitic nematode Radopholus similis. Mol. Plant Pathol. 2009, 10:389-401.
    • (2009) Mol. Plant Pathol. , vol.10 , pp. 389-401
    • Haegeman, A.1    Vanholme, B.2    Gheysen, G.3
  • 11
    • 0037780133 scopus 로고    scopus 로고
    • First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis
    • Larson S.B., Day J., Barba de la Rosa A.P., Keen N.T., McPherson A. First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis. Biochemistry 2003, 42:8411-8422.
    • (2003) Biochemistry , vol.42 , pp. 8411-8422
    • Larson, S.B.1    Day, J.2    Barba de la Rosa, A.P.3    Keen, N.T.4    McPherson, A.5
  • 12
    • 0030937787 scopus 로고    scopus 로고
    • Active-site motifs of lysosomal acid hydrolases: invariant features of clan GH-A glycosyl hydrolases deduced from hydrophobic cluster analysis
    • Durand P., Lehn P., Callebaut I., Fabrega S., Henrissat B., Mornon J.P. Active-site motifs of lysosomal acid hydrolases: invariant features of clan GH-A glycosyl hydrolases deduced from hydrophobic cluster analysis. Glycobiology 1997, 7:277-284.
    • (1997) Glycobiology , vol.7 , pp. 277-284
    • Durand, P.1    Lehn, P.2    Callebaut, I.3    Fabrega, S.4    Henrissat, B.5    Mornon, J.P.6
  • 13
    • 0030237081 scopus 로고    scopus 로고
    • Cloning and characterization of a xylanase gene from corn strains of Erwinia chrysanthemi
    • Keen N.T., Boyd C., Henrissat B. Cloning and characterization of a xylanase gene from corn strains of Erwinia chrysanthemi. Mol. Plant Microbe Interact. 1996, 9:651-657.
    • (1996) Mol. Plant Microbe Interact. , vol.9 , pp. 651-657
    • Keen, N.T.1    Boyd, C.2    Henrissat, B.3
  • 15
    • 70350436313 scopus 로고    scopus 로고
    • Crystal structure of the Salmonella enterica serovar typhimurium virulence factor SrfJ, a glycoside hydrolase family enzyme
    • Kim Y.G., Kim J.H., Kim K.J. Crystal structure of the Salmonella enterica serovar typhimurium virulence factor SrfJ, a glycoside hydrolase family enzyme. J. Bacteriol. 2009, 191:6550-6554.
    • (2009) J. Bacteriol. , vol.191 , pp. 6550-6554
    • Kim, Y.G.1    Kim, J.H.2    Kim, K.J.3
  • 16
    • 2142751536 scopus 로고    scopus 로고
    • Purification and charaterization of ginsenoside Ra-hydrolyzing beta-D-Xylosidase from Bifidobacterium breve K-110, a Human Intestinal Anaerobic Bacterium
    • Shin H.Y., Lee J.H., Lee J.Y., Han Y.O., Han M.J., Kim D.H. Purification and charaterization of ginsenoside Ra-hydrolyzing beta-D-Xylosidase from Bifidobacterium breve K-110, a Human Intestinal Anaerobic Bacterium. Biol. Pharm. Bull. 2003, 26:1170-1173.
    • (2003) Biol. Pharm. Bull. , vol.26 , pp. 1170-1173
    • Shin, H.Y.1    Lee, J.H.2    Lee, J.Y.3    Han, Y.O.4    Han, M.J.5    Kim, D.H.6
  • 17
    • 22144451852 scopus 로고    scopus 로고
    • BGN16.3, a novel acidic beta-1, 6-glucanase from mycoparasitic fungus Trichoderma harzianum CECT 2413
    • Montero M., Sanz L., Rey M., Monte E., Llobell A. BGN16.3, a novel acidic beta-1, 6-glucanase from mycoparasitic fungus Trichoderma harzianum CECT 2413. FEBS J. 2005, 272:3441-3448.
    • (2005) FEBS J. , vol.272 , pp. 3441-3448
    • Montero, M.1    Sanz, L.2    Rey, M.3    Monte, E.4    Llobell, A.5
  • 18
    • 33746410021 scopus 로고    scopus 로고
    • Functional analysis of an endo-1,6-beta-D-glucanase gene (neg-1) from Neurospora crassa
    • Oyama S., Inoue H., Yamagata Y., Nakajima T., Abe K. Functional analysis of an endo-1,6-beta-D-glucanase gene (neg-1) from Neurospora crassa. Biosci. Biotechnol. Biochem. 2006, 70:1773-1775.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 1773-1775
    • Oyama, S.1    Inoue, H.2    Yamagata, Y.3    Nakajima, T.4    Abe, K.5
  • 20
    • 0032896770 scopus 로고    scopus 로고
    • Pustulan-type polysaccharides as a constant character of the Umbilicariaceae (lichenized Ascomycotina)
    • Narui T., Sawada K., Culberson C.F., Culberson W.L., Shibata S. Pustulan-type polysaccharides as a constant character of the Umbilicariaceae (lichenized Ascomycotina). Bryologist 1999, 102:80-85.
    • (1999) Bryologist , vol.102 , pp. 80-85
    • Narui, T.1    Sawada, K.2    Culberson, C.F.3    Culberson, W.L.4    Shibata, S.5
  • 24
    • 0032512799 scopus 로고    scopus 로고
    • Empirical statistical estimates for sequence similarity searches
    • Pearson W.R. Empirical statistical estimates for sequence similarity searches. J. Mol. Biol. 1998, 276:71-84.
    • (1998) J. Mol. Biol. , vol.276 , pp. 71-84
    • Pearson, W.R.1
  • 26
    • 45949109669 scopus 로고    scopus 로고
    • MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences
    • Kumar S., Nei M., Dudley J., Tamura K. MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences. Brief. Bioinform. 2008, 9:299-306.
    • (2008) Brief. Bioinform. , vol.9 , pp. 299-306
    • Kumar, S.1    Nei, M.2    Dudley, J.3    Tamura, K.4
  • 27
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K., Misawa K., Kuma K., Miyata T. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res. 2002, 30:3059-3066.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 28
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987, 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 29
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon S., Gascuel O. A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol. 2003, 52:696-704.
    • (2003) Syst. Biol. , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 30
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • Guindon S., Dufayard J.F., Lefort V., Anisimova M., Hordijk W., Gascuel O. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst. Biol. 2010, 59:307-321.
    • (2010) Syst. Biol. , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 31
    • 33745256005 scopus 로고    scopus 로고
    • Approximate likelihood-ratio test for branches: a fast, accurate, and powerful alternative
    • Anisimova M., Gascuel O. Approximate likelihood-ratio test for branches: a fast, accurate, and powerful alternative. Syst. Biol. 2006, 55:539-552.
    • (2006) Syst. Biol. , vol.55 , pp. 539-552
    • Anisimova, M.1    Gascuel, O.2
  • 36
    • 12344324765 scopus 로고    scopus 로고
    • DIVAA: analysis of amino acid diversity in multiple aligned protein sequences
    • Rodi D.J., Mandava S., Makowski L. DIVAA: analysis of amino acid diversity in multiple aligned protein sequences. Bioinformatics 2004, 20:3481-3489.
    • (2004) Bioinformatics , vol.20 , pp. 3481-3489
    • Rodi, D.J.1    Mandava, S.2    Makowski, L.3
  • 37
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 39
    • 42349087940 scopus 로고    scopus 로고
    • Characterization of an endo-beta-1,6-Galactanase from Streptomyces avermitilis NBRC14893
    • Ichinose H., Kotake T., Tsumuraya Y., Kaneko S. Characterization of an endo-beta-1,6-Galactanase from Streptomyces avermitilis NBRC14893. Appl. Environ. Microbiol. 2008, 74:2379-2383.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 2379-2383
    • Ichinose, H.1    Kotake, T.2    Tsumuraya, Y.3    Kaneko, S.4
  • 40
    • 1242337328 scopus 로고    scopus 로고
    • Molecular cloning and expression in Escherichia coli of a Trichoderma viride endo-beta-(1→6)-galactanase gene
    • Kotake T., Kaneko S., Kubomoto A., Haque M.A., Kobayashi H., Tsumuraya Y. Molecular cloning and expression in Escherichia coli of a Trichoderma viride endo-beta-(1→6)-galactanase gene. Biochem. J. 2004, 377:749-755.
    • (2004) Biochem. J. , vol.377 , pp. 749-755
    • Kotake, T.1    Kaneko, S.2    Kubomoto, A.3    Haque, M.A.4    Kobayashi, H.5    Tsumuraya, Y.6
  • 41
    • 77952879995 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the novel acidic xylanase XYLD from Bispora sp. MEY-1 that is homologous to family 30 glycosyl hydrolases
    • Luo H., Yang J., Li J., Shi P., Huang H., Bai Y., Fan Y., Yao B. Molecular cloning and characterization of the novel acidic xylanase XYLD from Bispora sp. MEY-1 that is homologous to family 30 glycosyl hydrolases. Appl. Microbiol. Biotechnol. 2010, 86:1829-1839.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1829-1839
    • Luo, H.1    Yang, J.2    Li, J.3    Shi, P.4    Huang, H.5    Bai, Y.6    Fan, Y.7    Yao, B.8
  • 42
    • 0035101013 scopus 로고    scopus 로고
    • Functional characterization of a novel xylanase from a corn strain of Erwinia chrysanthemi
    • Hurlbert J.C., Preston J.F. Functional characterization of a novel xylanase from a corn strain of Erwinia chrysanthemi. J. Bacteriol. 2001, 183:2093-2100.
    • (2001) J. Bacteriol. , vol.183 , pp. 2093-2100
    • Hurlbert, J.C.1    Preston, J.F.2
  • 43
    • 0035542934 scopus 로고    scopus 로고
    • The (betaalpha)(8) glycosidases: sequence and structure analyses suggest distant evolutionary relationships
    • Nagano N., Porter C.T., Thornton J.M. The (betaalpha)(8) glycosidases: sequence and structure analyses suggest distant evolutionary relationships. Protein Eng. 2001, 14:845-855.
    • (2001) Protein Eng. , vol.14 , pp. 845-855
    • Nagano, N.1    Porter, C.T.2    Thornton, J.M.3
  • 44
    • 77956551236 scopus 로고    scopus 로고
    • Percentile-based spread: a more accurate way to compare crystallographic models
    • Pozharski E. Percentile-based spread: a more accurate way to compare crystallographic models. Acta Crystallogr. D Biol. Crystallogr. 2010, 66:970-978.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 970-978
    • Pozharski, E.1
  • 45
    • 0034308142 scopus 로고    scopus 로고
    • Practical limits of function prediction
    • Devos D., Valencia A. Practical limits of function prediction. Proteins 2000, 41:98-107.
    • (2000) Proteins , vol.41 , pp. 98-107
    • Devos, D.1    Valencia, A.2
  • 46
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost B. Twilight zone of protein sequence alignments. Protein. Eng. 1999, 12:85-94.
    • (1999) Protein. Eng. , vol.12 , pp. 85-94
    • Rost, B.1
  • 47
    • 0346799108 scopus 로고    scopus 로고
    • Prediction of protein function from protein sequence and structure
    • Whisstock J.C., Lesk A.M. Prediction of protein function from protein sequence and structure. Q. Rev. Biophys. 2003, 36:307-340.
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 307-340
    • Whisstock, J.C.1    Lesk, A.M.2
  • 49
    • 37249000280 scopus 로고    scopus 로고
    • Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum
    • Kitago Y., Karita S., Watanabe N., Kamiya M., Aizawa T., Sakka K., Tanaka I. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 2007, 282:35703-35711.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35703-35711
    • Kitago, Y.1    Karita, S.2    Watanabe, N.3    Kamiya, M.4    Aizawa, T.5    Sakka, K.6    Tanaka, I.7
  • 50
    • 33645559423 scopus 로고    scopus 로고
    • Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum
    • Taylor E.J., Smith N.L., Turkenburg J.P., D'Souza S., Gilbert H.J., Davies G.J. Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum. Biochem. J. 2006, 395:31-37.
    • (2006) Biochem. J. , vol.395 , pp. 31-37
    • Taylor, E.J.1    Smith, N.L.2    Turkenburg, J.P.3    D'Souza, S.4    Gilbert, H.J.5    Davies, G.J.6
  • 51
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: fine-tuning polysaccharide recognition
    • Boraston A.B., Bolam D.N., Gilbert H.J., Davies G.J. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 2004, 382:769-781.
    • (2004) Biochem. J. , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.