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Volumn 14, Issue 10, 2004, Pages 909-921

Processing enzyme glucosidase II: Proposed catalytic residues and developmental regulation during the ontogeny of the mouse mammary gland

Author keywords

Active site; Glucosidase II; Mammary gland

Indexed keywords

ACID; ASPARTIC ACID; BASE; COMPLEMENTARY DNA; GLUCOSE; GLUCOSIDASE; GLUTAMIC ACID; GLYCOPROTEIN; HYBRID PROTEIN; MANNOSE; MUTANT PROTEIN; N ACETYLNEURAMINIC ACID DERIVATIVE; NICKEL; OLIGOSACCHARIDE;

EID: 4644286883     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwh110     Document Type: Article
Times cited : (14)

References (32)
  • 1
    • 0030915788 scopus 로고    scopus 로고
    • Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II
    • Arendt, C.W. and Ostergaard, H.L. (1997) Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II. J. Biol. Chem., 272(20), 13117-13125.
    • (1997) J. Biol. Chem. , vol.272 , Issue.20 , pp. 13117-13125
    • Arendt, C.W.1    Ostergaard, H.L.2
  • 2
    • 0038187312 scopus 로고    scopus 로고
    • Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding
    • D'Alessio, C., Fernandez, F., Trombetta, E.S., and Parodi, A.J. (1999) Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding. J. Biol. Chem., 274(36), 25899-25905.
    • (1999) J. Biol. Chem. , vol.274 , Issue.36 , pp. 25899-25905
    • D'Alessio, C.1    Fernandez, F.2    Trombetta, E.S.3    Parodi, A.J.4
  • 3
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • Ellgaard, L. and Helenius, A. (2001) ER quality control: towards an understanding at the molecular level. Curr. Opin. Cell Biol., 13(4), 431-437.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , Issue.4 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 4
    • 0030836789 scopus 로고    scopus 로고
    • Expression of a cDNA encoding the glucose trimming enzyme glucosidase II in CHO cells and molecular characterization of the enzyme deficiency in a mutant mouse lymphoma cell line
    • Flura, T., Brada, D., Ziak, M., and Roth, J. (1997) Expression of a cDNA encoding the glucose trimming enzyme glucosidase II in CHO cells and molecular characterization of the enzyme deficiency in a mutant mouse lymphoma cell line. Glycobiology, 7(5), 617-624.
    • (1997) Glycobiology , vol.7 , Issue.5 , pp. 617-624
    • Flura, T.1    Brada, D.2    Ziak, M.3    Roth, J.4
  • 5
    • 0031972297 scopus 로고    scopus 로고
    • Plan α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin
    • Frandsen, T.P. and Svensson, B. (1998) Plan α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin. Plant Mol. Biol, 37, 1-13.
    • (1998) Plant Mol. Biol. , vol.37 , pp. 1-13
    • Frandsen, T.P.1    Svensson, B.2
  • 6
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Heleniuis, A. and Aebi, M. (2001) Intracellular functions of N-linked glycans. Science, 291, 2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Heleniuis, A.1    Aebi, M.2
  • 7
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat, B. and Davies, G. (1997) Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol., 7, 637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 8
    • 0029392961 scopus 로고
    • Families, superfamilies and subfamilies of glycosyl hydrolases
    • Henrissat, B. and Romeu, A. (1995) Families, superfamilies and subfamilies of glycosyl hydrolases. Biochem. J., 311, 350-351.
    • (1995) Biochem. J. , vol.311 , pp. 350-351
    • Henrissat, B.1    Romeu, A.2
  • 11
    • 0035405319 scopus 로고    scopus 로고
    • Milk lipid globules and their surrounding membranes: A brief history and perspectives for future research
    • Keenan, T.W. (2001) Milk lipid globules and their surrounding membranes: a brief history and perspectives for future research. J. Mammary Gland Biol. Neoplasia, 6, 365-371.
    • (2001) J. Mammary Gland Biol. Neoplasia , vol.6 , pp. 365-371
    • Keenan, T.W.1
  • 12
    • 0031180875 scopus 로고    scopus 로고
    • A catalytic amino acid and primary structure of active site in Aspergillus niger α-glucosidase
    • Kimura, A., Takata, M., Fukushi, Y., Mori, H., Natsui, H., and Chiba, S. (1997) A catalytic amino acid and primary structure of active site in Aspergillus niger α-glucosidase. Biosci. Biotechnol. Biochem., 61, 1091-1098.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1091-1098
    • Kimura, A.1    Takata, M.2    Fukushi, Y.3    Mori, H.4    Natsui, H.5    Chiba, S.6
  • 13
    • 0021891884 scopus 로고
    • Assembly of asparagines-linked oligosaccharides
    • Kornfeld, R. and Kornfeld, S. (1985) Assembly of asparagines-linked oligosaccharides. Anuu. Rev. Biochem., 54, 631-664.
    • (1985) Anuu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 14
    • 0018850985 scopus 로고
    • A simple, rapid, and sensitive DNA assay procedure
    • Labarca, C. and Paigen, K. (1980) A simple, rapid, and sensitive DNA assay procedure. Anal. Biochem, 102, 344-352.
    • (1980) Anal. Biochem. , vol.102 , pp. 344-352
    • Labarca, C.1    Paigen, K.2
  • 15
    • 0035887502 scopus 로고    scopus 로고
    • Identification of the catalytic nucleophile of the Family 31 alpha-glucosidase from Aspergillus niger via trapping of a 5-fluoroglycosyl-enzyme intermediate
    • Lee, S.S., He, S., and Withers, S.G. (2001) Identification of the catalytic nucleophile of the Family 31 alpha-glucosidase from Aspergillus niger via trapping of a 5-fluoroglycosyl-enzyme intermediate. Biochem. J., 359(2), 381-386.
    • (2001) Biochem. J. , vol.359 , Issue.2 , pp. 381-386
    • Lee, S.S.1    He, S.2    Withers, S.G.3
  • 16
    • 0022467150 scopus 로고
    • Immunolocalization of the oligosaccharide trimming enzyme glucosidase II
    • Lucocq, J.M., Brada, D., and Roth, J. (1986) Immunolocalization of the oligosaccharide trimming enzyme glucosidase II. J. Cell Biol., 102(6), 2137-2146.
    • (1986) J. Cell Biol. , vol.102 , Issue.6 , pp. 2137-2146
    • Lucocq, J.M.1    Brada, D.2    Roth, J.3
  • 18
    • 0028213490 scopus 로고
    • Glycosidases of the asparagines-linked oligosaccharide processing pathway
    • Moremen, K.W., Trimble, R.B., and Herscovics, A. (1994) Glycosidases of the asparagines-linked oligosaccharide processing pathway. Glycobiology, 4, 113-125.
    • (1994) Glycobiology , vol.4 , pp. 113-125
    • Moremen, K.W.1    Trimble, R.B.2    Herscovics, A.3
  • 19
    • 0035120194 scopus 로고    scopus 로고
    • Lactogenesis. The transition from pregnancy to lactation
    • Neville, M.C., Morton, J., and Umemura, S. (2001) Lactogenesis. The transition from pregnancy to lactation. Prediatr. Clin. North Am., 48, 35-52.
    • (2001) Prediatr. Clin. North Am. , vol.48 , pp. 35-52
    • Neville, M.C.1    Morton, J.2    Umemura, S.3
  • 21
    • 0017121125 scopus 로고
    • Partial amino acid sequence around the essential carboxylate in the active sites of the intestinal sucrose-isomaltase
    • Quaroni, A. and Semenza, G. (1976) Partial amino acid sequence around the essential carboxylate in the active sites of the intestinal sucrose-isomaltase. J. Biol. Chem., 251, 3250-3253.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3250-3253
    • Quaroni, A.1    Semenza, G.2
  • 22
    • 0028340566 scopus 로고
    • Developmental and hormonal regulation of UDP-GlcNAc:Dolichol phosphate GlcNAc-1-P transferase in mouse mammary gland
    • Rajput, B., Muniappa, N., and Vijay, I.K. (1994) Developmental and hormonal regulation of UDP-GlcNAc:dolichol phosphate GlcNAc-1-P transferase in mouse mammary gland. J. Biol. Chem., 269, 1-8.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-8
    • Rajput, B.1    Muniappa, N.2    Vijay, I.K.3
  • 24
    • 0023441662 scopus 로고
    • Purification and characterization of glucosidase II involved in N-linked glycoprotein processing in bovine mammary gland
    • Saxena, S., Shailubhai, K., Dong-Yu, B., and Vijay, I.K. (1987) Purification and characterization of glucosidase II involved in N-linked glycoprotein processing in bovine mammary gland. Biochem. J., 247(3), 563-570.
    • (1987) Biochem. J. , vol.247 , Issue.3 , pp. 563-570
    • Saxena, S.1    Shailubhai, K.2    Dong-Yu, B.3    Vijay, I.K.4
  • 25
    • 0028309453 scopus 로고
    • Identification of two aspartates and a glutamate essential for the activity of endo-beta-N-acetylglucosaminidase H from Streptomyces plicatus
    • Schmidt, B.F., Ashizawa, E., Jarnagin A.S., Lynn, S., Noto, G., Woodhouse, L., Estell, D.A., and Lad, P. (1994) Identification of two aspartates and a glutamate essential for the activity of endo-beta-N-acetylglucosaminidase H from Streptomyces plicatus. Arch Biochem Biophys., 311(2), 350-353.
    • (1994) Arch. Biochem. Biophys. , vol.311 , Issue.2 , pp. 350-353
    • Schmidt, B.F.1    Ashizawa, E.2    Jarnagin, A.S.3    Lynn, S.4    Noto, G.5    Woodhouse, L.6    Estell, D.A.7    Lad, P.8
  • 26
    • 0023444593 scopus 로고
    • Purification and characterization of glucosidase I involved in N-linked glycoprotein processing in bovine mammary gland
    • Shailubhai, K., Pratta, M.A., and Vijay, I.K. (1987) Purification and characterization of glucosidase I involved in N-linked glycoprotein processing in bovine mammary gland. Biochem. J., 247(3), 555-562.
    • (1987) Biochem. J. , vol.247 , Issue.3 , pp. 555-562
    • Shailubhai, K.1    Pratta, M.A.2    Vijay, I.K.3
  • 27
    • 0025287809 scopus 로고
    • Developmental regulation of glucosidase I, an enzyme involved in the processing of asparagines-linked glycoproteins in rat mammary gland
    • Shailubhai, K., Saxena, E.S., Balapures, A.K., and Vijay, I.K. (1990) Developmental regulation of glucosidase I, an enzyme involved in the processing of asparagines-linked glycoproteins in rat mammary gland. J. Biol. Chem., 265, 9701-9706.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9701-9706
    • Shailubhai, K.1    Saxena, E.S.2    Balapures, A.K.3    Vijay, I.K.4
  • 28
    • 0029910144 scopus 로고    scopus 로고
    • Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit
    • Trombetta, E.S., Simons, J.F., and Helenius A. (1996) Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem., 271(44), 27509-27516.
    • (1996) J. Biol. Chem. , vol.271 , Issue.44 , pp. 27509-27516
    • Trombetta, E.S.1    Simons, J.F.2    Helenius, A.3
  • 29
    • 0035807024 scopus 로고    scopus 로고
    • Quaternary and domain structure of glycoprotein processing glucosidase II
    • Trombetta E.S., Fleming K.G., and Helenius, A. (2001) Quaternary and domain structure of glycoprotein processing glucosidase II. Biochemistry, 40(35), 10717-10722.
    • (2001) Biochemistry , vol.40 , Issue.35 , pp. 10717-10722
    • Trombetta, E.S.1    Fleming, K.G.2    Helenius, A.3
  • 30
    • 0022508653 scopus 로고
    • Developmental regulation of glycosyltransferases involved in biosynthesis of asparagines-linked glycoproteins in mouse mammary gland
    • Vijay, I.K. and Oka, T. (1986) Developmental regulation of glycosyltransferases involved in biosynthesis of asparagines-linked glycoproteins in mouse mammary gland. Eur. J. Biochem., 154, 57-62.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 57-62
    • Vijay, I.K.1    Oka, T.2
  • 31
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity
    • Watanabe, T., Kobori, K., Miyashita, K., Fujii, T., Sakai, H., Uchida, M., and Tanaka, H. (1993) Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem., 268(25), 18567-18572.
    • (1993) J. Biol. Chem. , vol.268 , Issue.25 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Uchida, M.6    Tanaka, H.7
  • 32
    • 0028943508 scopus 로고
    • Approaches to labeling and identification of active site residues in glycosidases
    • Withers, S.G. and Aebersold, R. (1995) Approaches to labeling and identification of active site residues in glycosidases. Protein Sci., 4, 361-372.
    • (1995) Protein Sci. , vol.4 , pp. 361-372
    • Withers, S.G.1    Aebersold, R.2


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