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Volumn 38, Issue 3, 2004, Pages 463-476

Phylogenetic analysis of α-galactosidases of the GH27 family

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GALACTOSIDASE; DEXTRANASE; GLYCOSIDASE; GLYCOSIDE HYDROLASE 27 A ENZYME; GLYCOSIDE HYDROLASE 27 B ENZYME; GLYCOSIDE HYDROLASE 27 C ENZYME; GLYCOSIDE HYDROLASE 27 ENZYME; GLYCOSIDE HYDROLASE 36 ENZYME; ISOMALTODEXTRANASE ENZYME; UNCLASSIFIED DRUG;

EID: 6944235310     PISSN: 00268984     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (26)

References (36)
  • 1
    • 84888853384 scopus 로고    scopus 로고
    • Russian source
  • 2
    • 84888843758 scopus 로고    scopus 로고
    • Russian source
  • 3
    • 84888820554 scopus 로고    scopus 로고
    • Russian source
  • 4
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymatic glycosyl transfer
    • Sinnott M.L. 1990. Catalytic mechanisms of enzymatic glycosyl transfer. Chem. Rev. 90, 1171-1202.
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 5
    • 84888842462 scopus 로고    scopus 로고
    • Russian source
  • 6
    • 0032997597 scopus 로고    scopus 로고
    • Conserved sequence motifs in levansucrases and bifunctional β-xylosidases and α-L-arabinases
    • Naumoff D.G. 1999. Conserved sequence motifs in levansucrases and bifunctional β-xylosidases and α-L-arabinases. FEBS Lett. 448, 177-179.
    • (1999) FEBS Lett. , vol.448 , pp. 177-179
    • Naumoff, D.G.1
  • 7
    • 0035177354 scopus 로고    scopus 로고
    • β-fructosidase superfamily: Homology with some α-L-arabinases and β-D-xylosidases
    • Naumoff D.G. 2001. β-Fructosidase superfamily: homology with some α-L-arabinases and β-D-xylosidases. Protein Struct. Funct. Genet. 42, 66-76.
    • (2001) Protein Struct. Funct. Genet. , vol.42 , pp. 66-76
    • Naumoff, D.G.1
  • 8
    • 3042749528 scopus 로고    scopus 로고
    • Sequence analysis of glycosylhydrolases: β-fructosidase and α-galactosidase superfamilies
    • Naumoff D.G. 2001. Sequence analysis of glycosylhydrolases: β-fructosidase and α-galactosidase superfamilies. Glycoconjugate J. 18, 109.
    • (2001) Glycoconjugate J. , vol.18 , pp. 109
    • Naumoff, D.G.1
  • 9
    • 1042291218 scopus 로고    scopus 로고
    • Three acidic residues are at the active site of a β-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68
    • Pons T., Naumoff D.G., Martinez-Fleites C, Hernández L. 2004. Three acidic residues are at the active site of a β-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68. Protein Struct. Funct. Bioinform. 54, 424-432.
    • (2004) Protein Struct. Funct. Bioinform. , vol.54 , pp. 424-432
    • Pons, T.1    Naumoff, D.G.2    Martinez-Fleites, C.3    Hernández, L.4
  • 11
    • 0028810411 scopus 로고
    • Isolation and characterization of novel heterogeneous branched cyclomalto-oligosaccharides (cyclodextrins) produced by transgalactosylation with α-galactosidase from coffee bean
    • Koizumi K., Tanimoto T., Okada Y., Hara K., Fujita K., Hashimoto H., Kitahata S. 1995. Isolation and characterization of novel heterogeneous branched cyclomalto-oligosaccharides (cyclodextrins) produced by transgalactosylation with α-galactosidase from coffee bean. Carbohydr. Res. 278, 129-142.
    • (1995) Carbohydr. Res. , vol.278 , pp. 129-142
    • Koizumi, K.1    Tanimoto, T.2    Okada, Y.3    Hara, K.4    Fujita, K.5    Hashimoto, H.6    Kitahata, S.7
  • 12
    • 0031392412 scopus 로고    scopus 로고
    • Transglycosylation activity of α-D-galactosidase from Trichoderma reesei. An investigation of the active site
    • Eneyskaya E.V., Golubev A.M., Kachurin A.M., Savel'ev A.N., Neustroev K.N. 1998. Transglycosylation activity of α-D-galactosidase from Trichoderma reesei. An investigation of the active site. Carbohydr. Res. 305, 83-91.
    • (1998) Carbohydr. Res. , vol.305 , pp. 83-91
    • Eneyskaya, E.V.1    Golubev, A.M.2    Kachurin, A.M.3    Savel'Ev, A.N.4    Neustroev, K.N.5
  • 13
    • 0034693181 scopus 로고    scopus 로고
    • Comparative study of new α-galactosidases in transglycosylation reactions
    • Spangenberg P., Andre C., Dion M., Rabiller C., Mattes R. 2000. Comparative study of new α-galactosidases in transglycosylation reactions. Carbohydr. Res. 329, 65-73.
    • (2000) Carbohydr. Res. , vol.329 , pp. 65-73
    • Spangenberg, P.1    Andre, C.2    Dion, M.3    Rabiller, C.4    Mattes, R.5
  • 14
    • 2442419823 scopus 로고    scopus 로고
    • Purification and characterization of thermostable α-galactosidase from Ganoderma lucidum
    • Sripuan T., Aoki K., Yamamoto K., Tongkao D., Kumagai H. 2003. Purification and characterization of thermostable α-galactosidase from Ganoderma lucidum. Biosci. Biotechnol. Biochem. 67, 1485-1491.
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1485-1491
    • Sripuan, T.1    Aoki, K.2    Yamamoto, K.3    Tongkao, D.4    Kumagai, H.5
  • 15
    • 0036124422 scopus 로고    scopus 로고
    • The 1.9 Å structure of α-N-acetylgalactosaminidase: Molecular basis of glycosidase deficiency diseases
    • Garman S.C., Hannick L., Zhu A., Garboczi D.N. 2002. The 1.9 Å structure of α-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases. Structure. 10, 425-434.
    • (2002) Structure , vol.10 , pp. 425-434
    • Garman, S.C.1    Hannick, L.2    Zhu, A.3    Garboczi, D.N.4
  • 16
    • 0037827688 scopus 로고    scopus 로고
    • Crystal structure of rice α-galactosidase complexed with D-galactose
    • Fujimoto Z., Kaneko S., Momma M., Kobayashi H., Mizuno H. 2003. Crystal structure of rice α-galactosidase complexed with D-galactose. J. Biol. Chem. 278, 20313-20318.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20313-20318
    • Fujimoto, Z.1    Kaneko, S.2    Momma, M.3    Kobayashi, H.4    Mizuno, H.5
  • 18
    • 0037125202 scopus 로고    scopus 로고
    • Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13
    • Rigden D.J. 2002. Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13. FEBS Lett. 523, 17-22.
    • (2002) FEBS Lett. , vol.523 , pp. 17-22
    • Rigden, D.J.1
  • 19
    • 3042747192 scopus 로고    scopus 로고
    • α-galactosidase superfamily: Phylogenetic analysis and homology with some α-glucosidases
    • Groningen, The Netherlands. Abstract 32
    • Naumoff D.G. 2003. α-Galactosidase superfamily: phylogenetic analysis and homology with some α-glucosidases. Abstracts 5th Carbohydrate Bioengineering Meeting. Groningen, The Netherlands. P. 81. Abstract 32.
    • (2003) Abstracts 5th Carbohydrate Bioengineering Meeting , pp. 81
    • Naumoff, D.G.1
  • 20
    • 0034669589 scopus 로고    scopus 로고
    • α-galactosidase a from Pseudomonas fluorescens supsp. cellulosa: Cloning, high level expression and its role in galactomannan hydrolysis
    • Halstead J.R., Fransen M.P., Eberhart R.Y., Park A.J., Gilbert H.J., Hazlewood G.P. 2000. α-Galactosidase A from Pseudomonas fluorescens supsp. cellulosa: cloning, high level expression and its role in galactomannan hydrolysis. FEMS Microbiol. Lett. 192, 197-203.
    • (2000) FEMS Microbiol. Lett. , vol.192 , pp. 197-203
    • Halstead, J.R.1    Fransen, M.P.2    Eberhart, R.Y.3    Park, A.J.4    Gilbert, H.J.5    Hazlewood, G.P.6
  • 21
    • 0031680189 scopus 로고    scopus 로고
    • α-galactosidases of Penicillium simplicissimum: Production, purification and characterization of the gene encoding AGLI
    • Luonteri E., Alatalo E., Siika-aho M., Penttilä M., Tenkanen M. 1998. α-Galactosidases of Penicillium simplicissimum: production, purification and characterization of the gene encoding AGLI. Biotechnol. Appl. Biochem. 28, 179-188.
    • (1998) Biotechnol. Appl. Biochem. , vol.28 , pp. 179-188
    • Luonteri, E.1    Alatalo, E.2    Siika-aho, M.3    Penttilä, M.4    Tenkanen, M.5
  • 22
    • 0034669843 scopus 로고    scopus 로고
    • Purification and characterization of α-galactosidase from a thermophilic fungus Thermomyces lanuginosus
    • Puchart V., Vršanská M., Bhat M.K., Biely P. 2000. Purification and characterization of α-galactosidase from a thermophilic fungus Thermomyces lanuginosus. Biochim. Biophys. Acta. 1524, 27-37.
    • (2000) Biochim. Biophys. Acta. , vol.1524 , pp. 27-37
    • Puchart, V.1    Vršanská, M.2    Bhat, M.K.3    Biely, P.4
  • 23
    • 0034661436 scopus 로고    scopus 로고
    • Secondary structure and calcium-induced folding of the Clostridinm thermocellum dockerin domain determined by NMR spectroscopy
    • Lytle B.L., Volkman B.F., Westler W.M., Wu J.H.D. 2000. Secondary structure and calcium-induced folding of the Clostridinm thermocellum dockerin domain determined by NMR spectroscopy. Arch. Biochem. Biophys. 379, 237-244.
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 237-244
    • Lytle, B.L.1    Volkman, B.F.2    Westler, W.M.3    Wu, J.H.D.4
  • 25
    • 84888836026 scopus 로고    scopus 로고
    • Russian source
  • 27
    • 84888833035 scopus 로고    scopus 로고
    • Russian source
  • 28
    • 84888853266 scopus 로고    scopus 로고
    • Russian source
  • 29
    • 84888824705 scopus 로고    scopus 로고
    • Russian source
  • 32
    • 0034663962 scopus 로고    scopus 로고
    • Identification of Asp-130 as the catalytic nucleophile in the main α-galactosidase from Phanerochaete chrysosporium, a family 27 glycosyl hydrolase
    • Hart D.O., He S., Chany C.J., Withers S.G., Sims P.F., Sinnott M.L., Brumer H. 2000. Identification of Asp-130 as the catalytic nucleophile in the main α-galactosidase from Phanerochaete chrysosporium, a family 27 glycosyl hydrolase. Biochemistry. 39,9826-9836.
    • (2000) Biochemistry , vol.39 , pp. 9826-9836
    • Hart, D.O.1    He, S.2    Chany, C.J.3    Withers, S.G.4    Sims, P.F.5    Sinnott, M.L.6    Brumer, H.7
  • 33
    • 0034680672 scopus 로고    scopus 로고
    • The synthesis, testing and use of 5-fluoro-alpha-D-galactosyl fluoride to trap an intermediate on green coffee bean α-galactosidase and identify the catalytic nucleophile
    • Ly H.D., Howard S., Shum K., He S., Zhu A., Withers S.G. 2000. The synthesis, testing and use of 5-fluoro-alpha-D-galactosyl fluoride to trap an intermediate on green coffee bean α-galactosidase and identify the catalytic nucleophile. Carbohydr. Res. 329, 539-547.
    • (2000) Carbohydr. Res. , vol.329 , pp. 539-547
    • Ly, H.D.1    Howard, S.2    Shum, K.3    He, S.4    Zhu, A.5    Withers, S.G.6
  • 34
    • 0028935890 scopus 로고
    • Identification of tyrosine 108 in coffee bean α-galactosidase as an essential residue for the enzyme activity
    • Zhu A., Wang Z.K., Goldstein J. 1995. Identification of tyrosine 108 in coffee bean α-galactosidase as an essential residue for the enzyme activity. Biochim. Biophys. Acta. 1247, 260-264.
    • (1995) Biochim. Biophys. Acta. , vol.1247 , pp. 260-264
    • Zhu, A.1    Wang, Z.K.2    Goldstein, J.3
  • 35
    • 0030582405 scopus 로고    scopus 로고
    • Trp-16 is essential for the activity of α-galactosidase and α-N-acetylgalactosaminidase
    • Zhu A., Monahan C., Wang Z.K. 1996. Trp-16 is essential for the activity of α-galactosidase and α-N-acetylgalactosaminidase. Biochim. Biophys. Acta. 1297, 99-104.
    • (1996) Biochim. Biophys. Acta. , vol.1297 , pp. 99-104
    • Zhu, A.1    Monahan, C.2    Wang, Z.K.3
  • 36
    • 0034055714 scopus 로고    scopus 로고
    • Assessment of amino-acid substitutions at tryptophan 16 in α-galactosidase
    • Maranville E., Zhu A. 2000. Assessment of amino-acid substitutions at tryptophan 16 in α-galactosidase. Eur. J. Biochem. 267, 1495-1501.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1495-1501
    • Maranville, E.1    Zhu, A.2


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