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Volumn 8, Issue 3, 2010, Pages 437-451

GH101 family of glycoside hydrolases: Subfamily structure and evolutionary connections with other families

Author keywords

CAZy; Endo N acetylgalactosaminidase; Gene annotation; GH101; GH13; Glycoside hydrolases; Protein family; Protein phylogeny; PSI Protein Classifier; PSI BLAST; Sequence based classification of proteins; TIM barrel fold

Indexed keywords

GLYCOSIDASE;

EID: 77953678680     PISSN: 02197200     EISSN: None     Source Type: Journal    
DOI: 10.1142/S0219720010004628     Document Type: Conference Paper
Times cited : (15)

References (52)
  • 4
    • 27844482528 scopus 로고    scopus 로고
    • Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N-acetylgalactosaminidase from Bifidobacterium longum
    • Fujita K, Oura F, Nagamine N, Katayama T, Hiratake J, Sakata K, Kumagai H, Yamamoto K, Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N- acetylgalactosaminidase from Bifidobacterium longum, J Biol Chem 280(45):37415-37422, 2005.
    • (2005) J Biol Chem , vol.280 , Issue.45 , pp. 37415-37422
    • Fujita, K.1    Oura, F.2    Nagamine, N.3    Katayama, T.4    Hiratake, J.5    Sakata, K.6    Kumagai, H.7    Yamamoto, K.8
  • 5
    • 70350492958 scopus 로고    scopus 로고
    • Mechanistic investigation of the endo-α-N-acetylgalactosaminidase from Streptococcus pneumoniae R6
    • Willis LM, Zhang R, Reid A, Withers SG, Wakarchuk WW, Mechanistic investigation of the endo-α-N-acetylgalactosaminidase from Streptococcus pneumoniae R6, Biochemistry 48(43):10334-10341, 2009.
    • (2009) Biochemistry , vol.48 , Issue.43 , pp. 10334-10341
    • Willis, L.M.1    Zhang, R.2    Reid, A.3    Withers, S.G.4    Wakarchuk, W.W.5
  • 6
    • 0018632963 scopus 로고
    • Use of endo- and exoglycosidases for structural studies of glycoconjugates
    • Kobata A, Use of endo- and exoglycosidases for structural studies of glycoconjugates, Anal Biochem 100(1):l-14, 1979.
    • (1979) Anal Biochem , vol.100 , Issue.1
    • Kobata, A.1
  • 8
    • 0024331914 scopus 로고
    • Transglycosylation and transfer reaction activities of endo-α-N-acetyl-D-galactosaminidase from Diplococcus (Streptococcus) pneumoniae
    • Bardales RM, Bhavanandan VP, Transglycosylation and transfer reaction activities of endo-α-N-acetyl-D-galactosaminidase from Diplococcus (Streptococcus) pneumoniae, J Biol Chem 264(33):19893-19897, 1989.
    • (1989) J Biol Chem , vol.264 , Issue.33 , pp. 19893-19897
    • Bardales, R.M.1    Bhavanandan, V.P.2
  • 9
    • 0034650455 scopus 로고    scopus 로고
    • Characterization of endo-α-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity
    • Ashida H, Yamamoto K, Murata T, Usui T, Kumagai H, Characterization of endo-α-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity, Arch Biochem Biophys 373(2):394-400, 2000.
    • (2000) Arch Biochem Biophys , vol.373 , Issue.2 , pp. 394-400
    • Ashida, H.1    Yamamoto, K.2    Murata, T.3    Usui, T.4    Kumagai, H.5
  • 10
    • 0035961369 scopus 로고    scopus 로고
    • Enzymatic syntheses of T antigencontaining glycolipid mimicry using the transglycosylation activity of endo-α-Nacetylgalactosaminidase
    • Ashida H, Yamamoto K, Kumagai H, Enzymatic syntheses of T antigencontaining glycolipid mimicry using the transglycosylation activity of endo-α-Nacetylgalactosaminidase, Carbohydr Res 330(4):487-493, 2001.
    • (2001) Carbohydr Res , vol.330 , Issue.4 , pp. 487-493
    • Ashida, H.1    Yamamoto, K.2    Kumagai, H.3
  • 11
    • 0026568967 scopus 로고
    • Studies on the Thomsen-Friedenreich antigen in human colon with the lectin Amaranthin. Normal and neoplastic epithelium express only cryptic T antigen
    • Sata T, Roth J, Zuber C, Stamm B, Rinderle SJ, Goldstein IJ, Heitz PU, Studies on the Thomsen-Friedenreich antigen in human colon with the lectin Amaranthin. Normal and neoplastic epithelium express only cryptic T antigen, Lab Invest 66(2):175-186, 1992.
    • (1992) Lab Invest , vol.66 , Issue.2 , pp. 175-186
    • Sata, T.1    Roth, J.2    Zuber, C.3    Stamm, B.4    Rinderle, S.J.5    Goldstein, I.J.6    Heitz, P.U.7
  • 12
    • 70350455882 scopus 로고    scopus 로고
    • Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum
    • Suzuki R, Katayama T, Kitaoka M, Kumagai H, Wakagi T, Shoun H, Ashida H, Yamamoto K, Fushinobu S, Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum, J Biochem 146(3):389-398, 2009.
    • (2009) J Biochem , vol.146 , Issue.3 , pp. 389-398
    • Suzuki, R.1    Katayama, T.2    Kitaoka, M.3    Kumagai, H.4    Wakagi, T.5    Shoun, H.6    Ashida, H.7    Yamamoto, K.8    Fushinobu, S.9
  • 13
    • 77953673305 scopus 로고    scopus 로고
    • Release of O-glycans by enzymatic methods
    • Taniguchi N, Suzuki A, Ito Y, Narimatsu H, Kawasaki T, Hase S (eds.), Springer Japan
    • Iwase H, Release of O-glycans by enzymatic methods, Taniguchi N, Suzuki A, Ito Y, Narimatsu H, Kawasaki T, Hase S (eds.), Experimental Glycoscience, Springer Japan, 2008, pp.14-17.
    • (2008) Experimental Glycoscience , pp. 14-17
    • Iwase, H.1
  • 14
    • 0021106196 scopus 로고
    • Selective release of the disaccharide 2-acetamido-2- deoxy-3-O-(β-D- galactopyranosyl)-D-galactose from epiglycanin by endo-N-acetyl-α- D-galactosaminidase
    • Bhavanandan VP, Codington JF, Selective release of the disaccharide 2-acetamido-2- deoxy-3-O-(β-D-galactopyranosyl)-D-galactose from epiglycanin by endo-N-acetyl-α- D-galactosaminidase, Carbohydr Res 118:81-89, 1983.
    • (1983) Carbohydr Res , vol.118 , pp. 81-89
    • Bhavanandan, V.P.1    Codington, J.F.2
  • 15
    • 53049099530 scopus 로고    scopus 로고
    • Novel endo-α-N-acetylgalactosaminidases with broader substrate specificity
    • Koutsioulis D, Landry D, Guthrie EP, Novel endo-α-N- acetylgalactosaminidases with broader substrate specificity, Glycobiology 18(10):799-805, 2008.
    • (2008) Glycobiology , vol.18 , Issue.10 , pp. 799-805
    • Koutsioulis, D.1    Landry, D.2    Guthrie, E.P.3
  • 16
    • 0025290619 scopus 로고
    • Action of endo-α-N-acetylgalactosaminidase from Alcaligenes sp. on amino acid-Oglycans: Comparison with the enzyme from Diplococcus pneumoniae
    • Fan J-Q, Yamamoto K, Matsumoto Y, Hirabayashi Y, Kumagai H, Tochikura T, Action of endo-α-N-acetylgalactosaminidase from Alcaligenes sp. on amino acid-Oglycans: comparison with the enzyme from Diplococcus pneumoniae, Biochem Biophys Res Commun 169(2):751-757, 1990.
    • (1990) Biochem Biophys Res Commun , vol.169 , Issue.2 , pp. 751-757
    • Fan, J.-Q.1    Yamamoto, K.2    Matsumoto, Y.3    Hirabayashi, Y.4    Kumagai, H.5    Tochikura, T.6
  • 17
    • 85004485879 scopus 로고
    • Purification and characterization of endo-α-N- acetylgalactosaminidase from Alcaligenes sp
    • Fan J-Q, Kadowaki S, Yamamoto K, Kumagai H, Tochikura T, Purification and characterization of endo-α-N-acetylgalactosaminidase from Alcaligenes sp., Agric Biol Chem 52(7):1715-1723, 1988.
    • (1988) Agric Biol Chem , vol.52 , Issue.7 , pp. 1715-1723
    • Fan, J.-Q.1    Kadowaki, S.2    Yamamoto, K.3    Kumagai, H.4    Tochikura, T.5
  • 18
    • 85008745404 scopus 로고
    • Induction and efficient purification of endo-α-N- acetylgalactosaminidase from Alcaligenes sp
    • Fan J-Q, Yamamoto K, Kumagai H, Tochikura T, Induction and efficient purification of endo-α-N-acetylgalactosaminidase from Alcaligenes sp., Agric Biol Chem 54(1):233-234, 1990.
    • (1990) Agric Biol Chem , vol.54 , Issue.1 , pp. 233-234
    • Fan, J.-Q.1    Yamamoto, K.2    Kumagai, H.3    Tochikura, T.4
  • 19
    • 0005778326 scopus 로고
    • Isolation of endo-α- N-acetylgalactosaminidase from an aerobic bacterium
    • Yamamoto K, Fan J-Q, Kadowaki S, Kumagai H, Tochikura T, Isolation of endo-α- N-acetylgalactosaminidase from an aerobic bacterium, Agric Biol Chem 51(11):3169-3171, 1987.
    • (1987) Agric Biol Chem , vol.51 , Issue.11 , pp. 3169-3171
    • Yamamoto, K.1    Fan, J.-Q.2    Kadowaki, S.3    Kumagai, H.4    Tochikura, T.5
  • 20
    • 0025101071 scopus 로고
    • Isolation and characterization of major urinary amino acid O-glycosides and a dipeptide O-glycoside from a new lysosomal storage disorder (Kanzaki disease). Excessive excretion of serine- and threonine-linked glycan in the patient urine
    • Hirabayashi Y, Matsumoto Y, Matsumoto M, Toida T, Iida N, Matsubara T, Kanzaki T, Yokota M, Ishizuka I, Isolation and characterization of major urinary amino acid O-glycosides and a dipeptide O-glycoside from a new lysosomal storage disorder (Kanzaki disease). Excessive excretion of serine- and threonine-linked glycan in the patient urine, J Biol Chem 265(3):1693-1701, 1990.
    • (1990) J Biol Chem , vol.265 , Issue.3 , pp. 1693-1701
    • Hirabayashi, Y.1    Matsumoto, Y.2    Matsumoto, M.3    Toida, T.4    Iida, N.5    Matsubara, T.6    Kanzaki, T.7    Yokota, M.8    Ishizuka, I.9
  • 21
    • 21044451636 scopus 로고    scopus 로고
    • Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins
    • Katayama T, Fujita K, Yamamoto K, Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins, J Biosci Bioeng 99(5):457-465, 2005.
    • (2005) J Biosci Bioeng , vol.99 , Issue.5 , pp. 457-465
    • Katayama, T.1    Fujita, K.2    Yamamoto, K.3
  • 23
    • 77949275251 scopus 로고    scopus 로고
    • Syntheses of mucintype O-glycopeptides and oligosaccharides using transglycosylation and reversehydrolysis activities of Bifidobacterium endo-α-N-acetylgalactosaminidase
    • Ashida H, Ozawa H, Fujita K, Suzuki S, K. Yamamoto K, Syntheses of mucintype O-glycopeptides and oligosaccharides using transglycosylation and reversehydrolysis activities of Bifidobacterium endo-α-N- acetylgalactosaminidase, Glycoconj J 27(1):125-132, 2010.
    • (2010) Glycoconj J , vol.27 , Issue.1 , pp. 125-132
    • Ashida, H.1    Ozawa, H.2    Fujita, K.3    Suzuki, S.4    Yamamoto K, K.5
  • 24
    • 51449105672 scopus 로고    scopus 로고
    • Characterization of two different endo-α-Nacetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens
    • Ashida H, Maki R, Ozawa H, Tani Y, Kiyohara M, Fujita M, Imamura A, Ishida H, Kiso M, Yamamoto K, Characterization of two different endo-α-Nacetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens, Glycobiology 18(9):727-734, 2008.
    • (2008) Glycobiology , vol.18 , Issue.9 , pp. 727-734
    • Ashida, H.1    Maki, R.2    Ozawa, H.3    Tani, Y.4    Kiyohara, M.5    Fujita, M.6    Imamura, A.7    Ishida, H.8    Kiso, M.9    Yamamoto, K.10
  • 25
    • 0015502075 scopus 로고
    • Enzymes that destroy blood group specificity. V. The oligosaccharase of Clostridium perfringens
    • Huang CC, Aminoff D, Enzymes that destroy blood group specificity. V. The oligosaccharase of Clostridium perfringens, J Biol Chem 247(21): 6737-6742, 1972.
    • (1972) J Biol Chem , vol.247 , Issue.21 , pp. 6737-6742
    • Huang, C.C.1    Aminoff, D.2
  • 26
    • 0017083616 scopus 로고
    • Characterization of an endo-α-Nacetyl galactosaminidase from Diplococcus pneumoniae
    • Bhavanandan VP, Umemoto J, Davidson EA, Characterization of an endo-α-Nacetyl galactosaminidase from Diplococcus pneumoniae, Biochem Biophys Res Commun 70(3):738-745, 1976.
    • (1976) Biochem Biophys Res Commun , vol.70 , Issue.3 , pp. 738-745
    • Bhavanandan, V.P.1    Umemoto, J.2    Davidson, E.A.3
  • 29
    • 0017182324 scopus 로고
    • Partial purification and characterization of an endo-α- Nacetylgalactosaminidase from the culture of medium of Diplococcus pneumoniae
    • Endo Y, Kobata A, Partial purification and characterization of an endo-α-Nacetylgalactosaminidase from the culture of medium of Diplococcus pneumoniae, J Biochem 80(1):1-8, 1976.
    • (1976) J Biochem , vol.80 , Issue.1 , pp. 1-8
    • Endo, Y.1    Kobata, A.2
  • 30
    • 0017715417 scopus 로고
    • Systematic purification of five glycosidases from Streptococcus (Diplococcus) pneumoniae
    • Glasgow LR, Paulson JC, Hill RL, Systematic purification of five glycosidases from Streptococcus (Diplococcus) pneumoniae, J Biol Chem 252(23):8615-8623, 1977.
    • (1977) J Biol Chem , vol.252 , Issue.23 , pp. 8615-8623
    • Glasgow, L.R.1    Paulson, J.C.2    Hill, R.L.3
  • 31
    • 0017712481 scopus 로고
    • Purification and properties of an endo-α-N-acetyl-D- galactosaminidase from Diplococcus pneumoniae
    • Umemoto J, Bhavanandan VP, Davidson EA, Purification and properties of an endo-α-N-acetyl-D-galactosaminidase from Diplococcus pneumoniae, J Biol Chem 252(23):8609-8614, 1977.
    • (1977) J Biol Chem , vol.252 , Issue.23 , pp. 8609-8614
    • Umemoto, J.1    Bhavanandan, V.P.2    Davidson, E.A.3
  • 32
    • 0017833165 scopus 로고
    • Endo-α-Galactosidase and endo-α-N-acetylgalactosaminidase from Diplococcus pneumoniae
    • Kobata A, Takasaki S, endo-α-Galactosidase and endo-α-N- acetylgalactosaminidase from Diplococcus pneumoniae, Methods Enzymol 50:560-584, 1978.
    • (1978) Methods Enzymol , vol.50 , pp. 560-584
    • Kobata, A.1    Takasaki, S.2
  • 33
    • 0024331914 scopus 로고
    • Transglycosylation and transfer reaction activities of endo-α-N-acetyl-D-galactosaminidase from Diplococcus (Streptococcus) pneumoniae
    • Bardales RM, Bhavanandan VP, Transglycosylation and transfer reaction activities of endo-α-N-acetyl-D-galactosaminidase from Diplococcus (Streptococcus) pneumoniae, J Biol Chem 264(33):19893-19897, 1989.
    • (1989) J Biol Chem , vol.264 , Issue.33 , pp. 19893-19897
    • Bardales, R.M.1    Bhavanandan, V.P.2
  • 34
    • 0018124316 scopus 로고
    • Action of endo-α-N-acetyl- D-galactosaminidase on synthetic glycosides including chromogenic substrates
    • Umemoto J, Matta KL, Barlow JJ, Bhavanandan VP, Action of endo-α-N-acetyl- D-galactosaminidase on synthetic glycosides including chromogenic substrates, Anal Biochem 91(1):186-193, 1978.
    • (1978) Anal Biochem , vol.91 , Issue.1 , pp. 186-193
    • Umemoto, J.1    Matta, K.L.2    Barlow, J.J.3    Bhavanandan, V.P.4
  • 35
    • 0030946060 scopus 로고    scopus 로고
    • The substrate specificity of the enzyme endo-α-N-acetyl- Dgalactosaminidase from Diplococcus pneumonia
    • Brooks MM, Savage AV, The substrate specificity of the enzyme endo-α-N-acetyl-Dgalactosaminidase from Diplococcus pneumonia, Glycoconj J 14(2):183-190, 1997.
    • (1997) Glycoconj J , vol.14 , Issue.2 , pp. 183-190
    • Brooks, M.M.1    Savage, A.V.2
  • 36
    • 0024299248 scopus 로고
    • Release of oligosaccharides possessing reducing-end N-acetylgalactosamine from mucus glycoprotein in Streptomyces sp. OH-11242 culture medium through action of endo-type glycosidase
    • Iwase H, Ishii I, Ishihara K, Tanaka Y, Ømura S, Hotta K, Release of oligosaccharides possessing reducing-end N-acetylgalactosamine from mucus glycoprotein in Streptomyces sp. OH-11242 culture medium through action of endo-type glycosidase, Biochem Biophys Res Commun 151(1):422-428, 1988.
    • (1988) Biochem Biophys Res Commun , vol.151 , Issue.1 , pp. 422-428
    • Iwase, H.1    Ishii, I.2    Ishihara, K.3    Tanaka Ømura Y, S.4    Hotta, K.5
  • 37
    • 0026482984 scopus 로고
    • Partial purification and characterization of an endo-α-N- acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242
    • Ishii-Karakasa I, Iwase H, Hotta K, Tanaka Y, Omura S, Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242, Biochem J 288(2):475-482, 1992.
    • (1992) Biochem J , vol.288 , Issue.2 , pp. 475-482
    • Ishii-Karakasa, I.1    Iwase, H.2    Hotta, K.3    Tanaka, Y.4    Omura, S.5
  • 38
    • 0030808121 scopus 로고    scopus 로고
    • Structural determination of the O-linked sialyl oligosaccharides liberated from fetuin with endo-α-N-acetylgalactosaminidase-S by HPLC analysis and 600-MHz 1H-NMR spectroscopy
    • Ishii-Karakasa I, Iwase H, Hotta K, Structural determination of the O-linked sialyl oligosaccharides liberated from fetuin with endo-α-N- acetylgalactosaminidase-S by HPLC analysis and 600-MHz 1H-NMR spectroscopy, Eur J Biochem 247(2):709-715, 1997.
    • (1997) Eur J Biochem , vol.247 , Issue.2 , pp. 709-715
    • Ishii-Karakasa, I.1    Iwase, H.2    Hotta, K.3
  • 39
    • 0035348528 scopus 로고    scopus 로고
    • Efficient synthesis of O-linked glycopeptide by a transglycosylation using endo α-N-acetylgalactosaminidase from Streptomyces sp
    • Ajisaka K, Miyasato M, Ishii-Karakasa I, Efficient synthesis of O-linked glycopeptide by a transglycosylation using endo α-N- acetylgalactosaminidase from Streptomyces sp., Biosci Biotechnol Biochem 65(5):1240-1243, 2001.
    • (2001) Biosci Biotechnol Biochem , vol.65 , Issue.5 , pp. 1240-1243
    • Ajisaka, K.1    Miyasato, M.2    Ishii-Karakasa, I.3
  • 40
    • 0031925790 scopus 로고    scopus 로고
    • Screening and fermentation of endo-α-N-acetylgalactosaminidase S, a mucin-hydrolyzing enzyme from Streptomyces acting on the GalNAc-O-Ser (Thr) linkage
    • Tanaka Y, Takahashi Y, Shinose M, Ømura S, I.-Karakasa I, Iwase H, Hotta K, Screening and fermentation of endo-α-N-acetylgalactosaminidase S, a mucin-hydrolyzing enzyme from Streptomyces acting on the GalNAc-O-Ser (Thr) linkage, J Ferment Bioeng 85(4):381-387, 1998.
    • (1998) J Ferment Bioeng , vol.85 , Issue.4 , pp. 381-387
    • Tanaka, Y.1    Takahashi, Y.2    Shinose, M.3    Ømura, S.4    Karakasa, I.I.5    Iwase, H.6    Hotta, K.7
  • 41
    • 0027346353 scopus 로고
    • Release of O-linked glycoprotein glycans by endo-α- Nacetylgalactosaminidase
    • Iwase H, Hotta K, Release of O-linked glycoprotein glycans by endo-α-Nacetylgalactosaminidase, Methods Mol Biol 14:151-159, 1993.
    • (1993) Methods Mol Biol , vol.14 , pp. 151-159
    • Iwase, H.1    Hotta, K.2
  • 42
    • 57649134252 scopus 로고    scopus 로고
    • The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae: A target for structure-based vaccine design
    • Caines MEC, Zhu H, Vuckovic M, Willis LM, Withers SG, Wakarchuk WW, Strynadka NCJ, The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae: A target for structure-based vaccine design, J Biol Chem 283(46): 31279-31283, 2008.
    • (2008) J Biol Chem , vol.283 , Issue.46 , pp. 31279-31283
    • Mec, C.1    Zhu, H.2    Vuckovic, M.3    Willis, L.M.4    Withers, S.G.5    Wakarchuk, W.W.6    Ncj, S.7
  • 43
    • 59749100634 scopus 로고    scopus 로고
    • Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae
    • Gregg KJ, Boraston AB, Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae, Acta Crystallogr Sect F Struct Biol Cryst Commun 65(2):133-135, 2009.
    • (2009) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.65 , Issue.2 , pp. 133-135
    • Gregg, K.J.1    Boraston, A.B.2
  • 44
    • 70350751665 scopus 로고    scopus 로고
    • New program PSI Protein Classifier automatizes the PSIBLAST results analysis
    • Naumoff DG, Carreras M, New program PSI Protein Classifier automatizes the PSIBLAST results analysis, Molecular Biology (Engl. Transl.) 43(4):652-664, 2009.
    • (2009) Molecular Biology (Engl. Transl. , vol.43 , Issue.4 , pp. 652-664
    • Naumoff, D.G.1    Carreras, M.2
  • 46
    • 77953669891 scopus 로고    scopus 로고
    • Proceedings of the International Moscow Conference on Computational Molecular Biology (MCCMB'09)
    • July 20-23 2009, Moscow, Russia
    • Naumoff DG, Sequence analysis of endo-α-N-acetylgalactosaminidases and their homologues, Proceedings of the International Moscow Conference on Computational Molecular Biology (MCCMB'09), July 20-23, 2009, Moscow, Russia, pp.251-252, 2009 (http://mccmb.belozersky.msu.ru/2009/MCCMB09 Proceedings.pdf).
    • (2009) Sequence Analysis of Endo-α-N-acetylgalactosaminidases and Their Homologues , pp. 251-252
    • Naumoff, D.G.1
  • 47
    • 77953659911 scopus 로고    scopus 로고
    • Sequence analysis of endo-α-N-acetylgalactosaminidases, (Abstracts of 20th International Symposium on Glycoconjugates "gLYCO XX"
    • November 29 - December 4, 2009, San Juan, Puerto Rico, USA
    • Naumoff DG, Sequence analysis of endo-α-N-acetylgalactosaminidases, (Abstracts of 20th International Symposium on Glycoconjugates "GLYCO XX", November 29 - December 4, 2009, San Juan, Puerto Rico, USA), Glycoconj J 26(7):847, 2009.
    • (2009) Glycoconj J , vol.26 , Issue.7 , pp. 847
    • Naumoff, D.G.1
  • 49
    • 70350786081 scopus 로고    scopus 로고
    • The GH31 family of glycoside hydrolases: Subfamily structure and evolutionary connections, Abstracts
    • June 22- 28 2008, Novosibirsk, Russia
    • Naumoff DG, The GH31 family of glycoside hydrolases: subfamily structure and evolutionary connections, Abstracts. The Sixth International Conference on Bioinformatics of Genome Regulation and Structure (BGRS'2008), June 22- 28, 2008, Novosibirsk, Russia, pp.169, 2008 (http://www.bionet.nsc.ru/meeting/ bgrs2008/BGRS2008 Proceedings.pdf).
    • (2008) The Sixth International Conference on Bioinformatics of Genome Regulation and Structure (BGRS'2008) , pp. 169
    • Naumoff, D.G.1
  • 50
    • 6944235310 scopus 로고    scopus 로고
    • Phylogenetic analysis of α-galactosidases of the GH27 family
    • Naumoff DG, Phylogenetic analysis of α-galactosidases of the GH27 family, Molecular Biology (Engl. Transl.) 38(3):388-399, 2004.
    • (2004) Molecular Biology (Engl. Transl. , vol.38 , Issue.3 , pp. 388-399
    • Naumoff, D.G.1
  • 51
    • 26844441931 scopus 로고    scopus 로고
    • Analysis of glycoside hydrolase family 98: Catalytic machinery, mechanism and a novel putative carbohydrate binding module
    • Rigden DJ, Analysis of glycoside hydrolase family 98: catalytic machinery, mechanism and a novel putative carbohydrate binding module, FEBS Lett 579(25):5466-5472, 2005.
    • (2005) FEBS Lett , vol.579 , Issue.25 , pp. 5466-5472
    • Rigden, D.J.1
  • 52
    • 77953658963 scopus 로고    scopus 로고
    • The Pfam database. Pfam 24.0. (2009) (http://pfam.sanger.ac.uk).
    • (2009) The Pfam Database


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