메뉴 건너뛰기




Volumn 71, Issue 7, 2007, Pages 1626-1635

Molecular cloning and expression of two novel β-N- acetylglucosaminidases from silkworm Bombyx mori

Author keywords

N acetylglucosaminidase; Bombyx mori; Glycosylhydrolase

Indexed keywords

BIOSYNTHESIS; CLONING; DEGRADATION; DNA; GENES; GLYCOPROTEINS; PHYSIOLOGY;

EID: 34548459371     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60705     Document Type: Article
Times cited : (32)

References (28)
  • 2
    • 0032059448 scopus 로고    scopus 로고
    • Glycosidase families
    • Henrissat, B., Glycosidase families. Biochem. Soc. Trans., 26, 153-156 (1998).
    • (1998) Biochem. Soc. Trans , vol.26 , pp. 153-156
    • Henrissat, B.1
  • 3
    • 0027561440 scopus 로고
    • Insect cell hosts for baculovirus expression vectors contain endogenous exoglycosidase activity
    • Licari, P. J., Jarvis, D. L., and Bailey, J. E., Insect cell hosts for baculovirus expression vectors contain endogenous exoglycosidase activity. Biotechnol. Prog., 9, 146-152 (1993).
    • (1993) Biotechnol. Prog , vol.9 , pp. 146-152
    • Licari, P.J.1    Jarvis, D.L.2    Bailey, J.E.3
  • 5
    • 85007732820 scopus 로고
    • Purification of a chitooligosaccharidolytic β-N- acetylglucosaminidase from Bombyx mori larvae during metamorphosis and the nucleotide sequence of its cDNA
    • Nagamatsu, Y., Yanagisawa, I., Kimoto, M., Okamoto, E., and Koga, D., Purification of a chitooligosaccharidolytic β-N- acetylglucosaminidase from Bombyx mori larvae during metamorphosis and the nucleotide sequence of its cDNA. Biosci. Biotechnol. Biochem., 59, 219-225 (1995).
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , pp. 219-225
    • Nagamatsu, Y.1    Yanagisawa, I.2    Kimoto, M.3    Okamoto, E.4    Koga, D.5
  • 6
    • 0005303743 scopus 로고
    • Metabolic conversions during putation of the cecropia silkworm. 1. Deposition and utilization of nutrient reserves
    • Bade, M. L., and Wyatt, G. R., Metabolic conversions during putation of the cecropia silkworm. 1. Deposition and utilization of nutrient reserves. Biochem. J., 83, 470-478 (1962).
    • (1962) Biochem. J , vol.83 , pp. 470-478
    • Bade, M.L.1    Wyatt, G.R.2
  • 7
    • 0001748976 scopus 로고
    • Cuticle secretion during larval growth in Drosophila melanogaster
    • Kaznowski, C., Schneiderman, H. A., and Bryant, P. J., Cuticle secretion during larval growth in Drosophila melanogaster. J. Insect Physiol., 31, 801-813 (1985).
    • (1985) J. Insect Physiol , vol.31 , pp. 801-813
    • Kaznowski, C.1    Schneiderman, H.A.2    Bryant, P.J.3
  • 8
    • 0029085691 scopus 로고
    • Insect cells contain an unusual, membrane-bound β-N- acetylglucosaminidase probably involved in the processing of protein N-glycans
    • Altmann, F., Schwihla, H., Staudacher, E., Glossl, J., and Marz, L., Insect cells contain an unusual, membrane-bound β-N- acetylglucosaminidase probably involved in the processing of protein N-glycans. J. Biol. Chem., 270, 17344-17349 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 17344-17349
    • Altmann, F.1    Schwihla, H.2    Staudacher, E.3    Glossl, J.4    Marz, L.5
  • 9
    • 0034855620 scopus 로고    scopus 로고
    • Male sterile mutant casanova gives clues to mechanisms of sperm-egg interactions in Drosophila melanogaster
    • Perotti, M. E., Cattaneo, F., Pasini, M. E., Verni, F., and Hackstein, J. H., Male sterile mutant casanova gives clues to mechanisms of sperm-egg interactions in Drosophila melanogaster. Mol. Reprod. Dev., 60, 248-259 (2001).
    • (2001) Mol. Reprod. Dev , vol.60 , pp. 248-259
    • Perotti, M.E.1    Cattaneo, F.2    Pasini, M.E.3    Verni, F.4    Hackstein, J.H.5
  • 10
    • 0035983294 scopus 로고    scopus 로고
    • Purification and characterization of the plasma membrane glycosidases of Drosophila melanogaster spermatozoa
    • Cattaneo, F., Ogiso, M., Hoshi, M., Perotti, M. E., and Pasini, M. E., Purification and characterization of the plasma membrane glycosidases of Drosophila melanogaster spermatozoa. Insect Biochem. Mol. Biol., 32, 929-941 (2002).
    • (2002) Insect Biochem. Mol. Biol , vol.32 , pp. 929-941
    • Cattaneo, F.1    Ogiso, M.2    Hoshi, M.3    Perotti, M.E.4    Pasini, M.E.5
  • 11
    • 33748703846 scopus 로고    scopus 로고
    • Identification and expression analysis of Drosophila melanogaster genes encoding β-hexosaminidases of the sperm plasma membrane
    • Cattaneo, F., Pasini, M. E., Intra, J., Matsumoto, M., Briani, F., Hoshi, M., and Perotti, M. E., Identification and expression analysis of Drosophila melanogaster genes encoding β-hexosaminidases of the sperm plasma membrane. Glycobiology, 16, 786-800 (2006).
    • (2006) Glycobiology , vol.16 , pp. 786-800
    • Cattaneo, F.1    Pasini, M.E.2    Intra, J.3    Matsumoto, M.4    Briani, F.5    Hoshi, M.6    Perotti, M.E.7
  • 12
    • 33646178162 scopus 로고    scopus 로고
    • The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing
    • Leonard, R., Rendic, D., Rabouille, C., Wilson, I. B., Preat, T., and Altmann, F., The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing. J. Biol. Chem., 281, 4867-4875 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 4867-4875
    • Leonard, R.1    Rendic, D.2    Rabouille, C.3    Wilson, I.B.4    Preat, T.5    Altmann, F.6
  • 13
    • 33646585194 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of β-N-acetylglucosaminidase genes from Sf9 cells
    • Aumiller, J. J., Hollister, J. R., and Jarvis, D. L., Molecular cloning and functional characterization of β-N-acetylglucosaminidase genes from Sf9 cells. Protein Expr. Purif., 47, 571-590 (2005).
    • (2005) Protein Expr. Purif , vol.47 , pp. 571-590
    • Aumiller, J.J.1    Hollister, J.R.2    Jarvis, D.L.3
  • 15
    • 0028236119 scopus 로고
    • Structures of the N-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N)
    • Kubelka, V., Altmann, F., Kornfeld, G., and Marz, L., Structures of the N-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N). Arch. Biochem. Biophys., 308, 148-157 (1994).
    • (1994) Arch. Biochem. Biophys , vol.308 , pp. 148-157
    • Kubelka, V.1    Altmann, F.2    Kornfeld, G.3    Marz, L.4
  • 16
    • 0025882349 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch, A., PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res., 19, 2241-2245 (1991).
    • (1991) Nucleic Acids Res , vol.19 , pp. 2241-2245
    • Bairoch, A.1
  • 17
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer, E. L., Eddy, S. R., and Durbin, R., Pfam: a comprehensive database of protein domain families based on seed alignments. Proteins, 28, 405-420 (1997).
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 18
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • Hirokawa, T., Boon-Chieng, S., and Mitaku, S., SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics, 14, 378-379 (1998).
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 20
    • 0021308647 scopus 로고
    • Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins
    • Hase, S., Ibuki, T., and Ikenaka, T., Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins. J. Biochem. (Tokyo), 95, 197-203 (1984).
    • (1984) J. Biochem. (Tokyo) , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 21
    • 0014199519 scopus 로고
    • Studies on the glycosidases in jack bean meal. I. Isolation and properties of α-mannosidase
    • Li, Y. T., Studies on the glycosidases in jack bean meal. I. Isolation and properties of α-mannosidase. J. Biol. Chem., 242, 5474-5480 (1967).
    • (1967) J. Biol. Chem , vol.242 , pp. 5474-5480
    • Li, Y.T.1
  • 22
    • 0020687572 scopus 로고
    • β-D-mannosidase from Helix pomatia
    • McCleary, B. V., β-D-mannosidase from Helix pomatia. Carbohydr. Res., 111, 297-310 (1983).
    • (1983) Carbohydr. Res , vol.111 , pp. 297-310
    • McCleary, B.V.1
  • 24
    • 0034647424 scopus 로고    scopus 로고
    • Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-D-glucosamine: The catalytic role of the conserved acidic pair, aspertate 539 and glutamate 540
    • Prag, G., Papanikolau, Y., Tavlas, G., Vorgias, C. E., Petratos, K., and Oppenheim, A. B., Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-D-glucosamine: the catalytic role of the conserved acidic pair, aspertate 539 and glutamate 540. J. Mol. Biol., 300, 611-617 (2000).
    • (2000) J. Mol. Biol , vol.300 , pp. 611-617
    • Prag, G.1    Papanikolau, Y.2    Tavlas, G.3    Vorgias, C.E.4    Petratos, K.5    Oppenheim, A.B.6
  • 25
    • 33744798282 scopus 로고    scopus 로고
    • Crystallographic structure of human β-hexosaminidase A: Interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis
    • Lemieux, M. J., Mark, B. L., Cherney, M. M., Withers, S. G., Mahuran, D. J., and James, M. N., Crystallographic structure of human β-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis. J. Mol. Biol., 359, 913-929 (2006).
    • (2006) J. Mol. Biol , vol.359 , pp. 913-929
    • Lemieux, M.J.1    Mark, B.L.2    Cherney, M.M.3    Withers, S.G.4    Mahuran, D.J.5    James, M.N.6
  • 26
    • 0344837327 scopus 로고    scopus 로고
    • Crystal structure of human β-hexosaminidase B: Understanding the molecular basis of Sandhoff and Tay-Sachs disease
    • Mark, B. L., Mahuran, D. J., Cherney, M. M., Zhao, D., Knapp, S., and James, M. N. G., Crystal structure of human β-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease. J. Mol. Biol., 327, 1093-1109 (2003).
    • (2003) J. Mol. Biol , vol.327 , pp. 1093-1109
    • Mark, B.L.1    Mahuran, D.J.2    Cherney, M.M.3    Zhao, D.4    Knapp, S.5    James, M.N.G.6
  • 27
    • 0029940470 scopus 로고    scopus 로고
    • Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs desease
    • Tews, I., Perrakis, A., Oppenheim, A., Dauter, Z., Wilson, K. S., and Vorgias, C. E., Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs desease. Nat. Struct. Biol., 3, 638-648 (1996).
    • (1996) Nat. Struct. Biol , vol.3 , pp. 638-648
    • Tews, I.1    Perrakis, A.2    Oppenheim, A.3    Dauter, Z.4    Wilson, K.S.5    Vorgias, C.E.6
  • 28
    • 0037131312 scopus 로고    scopus 로고
    • Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state
    • Williams, S. J., Mark, B. L., Vocadlo, D. J., James, M. N., and Withers, S. G., Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. J. Biol. Chem., 277, 40055-40065 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 40055-40065
    • Williams, S.J.1    Mark, B.L.2    Vocadlo, D.J.3    James, M.N.4    Withers, S.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.