메뉴 건너뛰기




Volumn 23, Issue 6, 2013, Pages 736-744

Identification and characterization of endo-β-N-acetylglucosaminidase from methylotrophic yeast Ogataea minuta

Author keywords

Endo N acetylglucosaminidase; Endo Om; Ogataea minuta; transglycosylation; yeast

Indexed keywords

AMINO ACID; GENOMIC DNA; GLYCAN DERIVATIVE; GLYCOSIDASE; GLYCOSIDE HYDROLASE FAMILY 85; MANNOSE; N ACETYL BETA GLUCOSAMINIDASE; N ACETYLGLUCOSAMINE; OLIGOSACCHARIDE; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 84877258611     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwt012     Document Type: Article
Times cited : (41)

References (36)
  • 1
    • 66449099328 scopus 로고    scopus 로고
    • Streptococcus pneumoniae endohexosaminidase D, structural and mechanistic insight into substrate-assisted catalysis in family 85 glycoside hydrolases
    • Abbott DW, Macauley MS, Vocadlo DJ, Boraston AB. 2009. Streptococcus pneumoniae endohexosaminidase D, structural and mechanistic insight into substrate-assisted catalysis in family 85 glycoside hydrolases. J Biol Chem. 284:11676-11689.
    • (2009) J Biol Chem , vol.284 , pp. 11676-11689
    • Abbott, D.W.1    MacAuley, M.S.2    Vocadlo, D.J.3    Boraston, A.B.4
  • 2
    • 0042068176 scopus 로고    scopus 로고
    • Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: Roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p)
    • Chantret I, Frénoy JP, Moore SE. 2003. Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: Roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p). Biochem J. 373:901-908.
    • (2003) Biochem J , vol.373 , pp. 901-908
    • Chantret, I.1    Frénoy, J.P.2    Moore, S.E.3
  • 3
    • 40549122304 scopus 로고    scopus 로고
    • Free oligosaccharide regulation during mammalian protein N-glycosylation
    • Chantret I, Moore SE. 2008. Free oligosaccharide regulation during mammalian protein N-glycosylation. Glycobiology. 18:210-224.
    • (2008) Glycobiology , vol.18 , pp. 210-224
    • Chantret, I.1    Moore, S.E.2
  • 4
    • 0035875889 scopus 로고    scopus 로고
    • EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG
    • Collin M, Olsén A. 2001. EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG. EMBO J. 20:3046-3055.
    • (2001) EMBO J , vol.20 , pp. 3046-3055
    • Collin, M.1    Olsén, A.2
  • 5
    • 80052620508 scopus 로고    scopus 로고
    • The two endo-β-N-acetylglucosaminidase genes from Arabidopsis thaliana encode cytoplasmic enzymes controlling free N-glycan levels
    • Fischl RM, Stadlmann J, Grass J, Altmann F, Léonard R. 2011. The two endo-β-N-acetylglucosaminidase genes from Arabidopsis thaliana encode cytoplasmic enzymes controlling free N-glycan levels. Plant Mol Biol. 77:275-284.
    • (2011) Plant Mol Biol , vol.77 , pp. 275-284
    • Fischl, R.M.1    Stadlmann, J.2    Grass, J.3    Altmann, F.4    Léonard, R.5
  • 6
    • 0026799211 scopus 로고
    • N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardmentmass spectrometry, and 1H nuclear magnetic resonance spectroscopy
    • Fu D, van Halbeek H. 1992. N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardmentmass spectrometry, and 1H nuclear magnetic resonance spectroscopy. Anal Biochem. 206:53-63.
    • (1992) Anal Biochem , vol.206 , pp. 53-63
    • Fu, D.1    Van Halbeek, H.2
  • 7
    • 7044274809 scopus 로고    scopus 로고
    • Molecular cloning of Mucor hiemalis endo-β-N- acetylglucosaminidase and some properties of the recombinant enzyme
    • Fujita K, Kobayashi K, Iwamatsu A, Takeuchi M, Kumagai H, Yamamoto K. 2004. Molecular cloning of Mucor hiemalis endo-β-N- acetylglucosaminidase and some properties of the recombinant enzyme. Arch Biochem Biophys. 432:41-49.
    • (2004) Arch Biochem Biophys , vol.432 , pp. 41-49
    • Fujita, K.1    Kobayashi, K.2    Iwamatsu, A.3    Takeuchi, M.4    Kumagai, H.5    Yamamoto, K.6
  • 8
    • 4544289558 scopus 로고    scopus 로고
    • Characterization of endo-β-N-acetylglucosaminidase from alkaliphilic Bacillus halodurans C-125
    • Fujita K, Takami H, Yamamoto K, Takegawa K. 2004. Characterization of endo-β-N-acetylglucosaminidase from alkaliphilic Bacillus halodurans C-125. Biosci Biotechnol Biochem. 68:1059-1066.
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 1059-1066
    • Fujita, K.1    Takami, H.2    Yamamoto, K.3    Takegawa, K.4
  • 9
    • 68749109521 scopus 로고    scopus 로고
    • Establishment of a real-time analytical method for free oligosaccharide transport from the ER to the cytosol
    • Haga Y, Totani K, Ito Y, Suzuki T. 2009. Establishment of a real-time analytical method for free oligosaccharide transport from the ER to the cytosol. Glycobiology. 19:987-994.
    • (2009) Glycobiology , vol.19 , pp. 987-994
    • Haga, Y.1    Totani, K.2    Ito, Y.3    Suzuki, T.4
  • 10
    • 77952295841 scopus 로고    scopus 로고
    • Purification, characterization and molecular cloning of a novel endo-β-N-acetylglucosaminidase from the basidiomycete, Flammulina velutipes
    • Hamaguchi T, Ito T, Inoue Y, Limpaseni T, Pongsawasdi P, Ito K. 2010. Purification, characterization and molecular cloning of a novel endo-β-N-acetylglucosaminidase from the basidiomycete, Flammulina velutipes. Glycobiology. 20:420-432.
    • (2010) Glycobiology , vol.20 , pp. 420-432
    • Hamaguchi, T.1    Ito, T.2    Inoue, Y.3    Limpaseni, T.4    Pongsawasdi, P.5    Ito, K.6
  • 11
    • 77951228197 scopus 로고    scopus 로고
    • Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae
    • Hirayama H, Seino J, Kitajima T, Jigami Y, Suzuki T. 2010. Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae. J Biol Chem. 285:12390-12404.
    • (2010) J Biol Chem , vol.285 , pp. 12390-12404
    • Hirayama, H.1    Seino, J.2    Kitajima, T.3    Jigami, Y.4    Suzuki, T.5
  • 12
    • 84864238717 scopus 로고    scopus 로고
    • Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions
    • Huang W, Giddens J, Fan SQ, Toonstra C, Wang LX. 2012. Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions. J Am Chem Soc. 134:12308-12318.
    • (2012) J Am Chem Soc , vol.134 , pp. 12308-12318
    • Huang, W.1    Giddens, J.2    Fan, S.Q.3    Toonstra, C.4    Wang, L.X.5
  • 13
    • 0036798689 scopus 로고    scopus 로고
    • Identification of an endo-β-N-acetylglucosaminidase gene in Caenorhabditis elegans and its expression in Escherichia coli
    • Kato T, Fujita K, Takeuchi M, Kobayashi K, Natsuka S, Ikura K, Kumagai H, Yamamoto K. 2002. Identification of an endo-β-N-acetylglucosaminidase gene in Caenorhabditis elegans and its expression in Escherichia coli. Glycobiology. 12:581-587.
    • (2002) Glycobiology , vol.12 , pp. 581-587
    • Kato, T.1    Fujita, K.2    Takeuchi, M.3    Kobayashi, K.4    Natsuka, S.5    Ikura, K.6    Kumagai, H.7    Yamamoto, K.8
  • 14
    • 34547604159 scopus 로고    scopus 로고
    • Free oligosaccharides in the cytosol of Caenorhabditis elegans are generated through endoplasmic reticulum-Golgi trafficking
    • Kato T, Kitamura K, Maeda M, Kimura Y, Katayama T, Ashida H, Yamamoto K. 2007. Free oligosaccharides in the cytosol of Caenorhabditis elegans are generated through endoplasmic reticulum-Golgi trafficking. J Biol Chem. 282:22080-22088.
    • (2007) J Biol Chem , vol.282 , pp. 22080-22088
    • Kato, T.1    Kitamura, K.2    Maeda, M.3    Kimura, Y.4    Katayama, T.5    Ashida, H.6    Yamamoto, K.7
  • 17
    • 33750025988 scopus 로고    scopus 로고
    • Production of Man5GlcNAc2-type sugar chain by the methylotrophic yeast Ogataea minuta
    • Kuroda K, Kobayashi K, Tsumura H, Komeda T, Chiba Y, Jigami Y. 2006. Production of Man5GlcNAc2-type sugar chain by the methylotrophic yeast Ogataea minuta. FEMS Yeast Res. 6:1052-1062.
    • (2006) FEMS Yeast Res , vol.6 , pp. 1052-1062
    • Kuroda, K.1    Kobayashi, K.2    Tsumura, H.3    Komeda, T.4    Chiba, Y.5    Jigami, Y.6
  • 18
    • 67349093886 scopus 로고    scopus 로고
    • The X-ray crystal structure of an Arthrobacter protophormiae endo-β-N-acetylglucosaminidase reveals a (β/α)8 catalytic domain, two ancillary domains and active site residues key for transglycosylation activity
    • Ling Z, Suits MD, Bingham RJ, Bruce NC, Davies GJ, Fairbanks AJ, Moir JW, Taylor EJ. 2009. The X-ray crystal structure of an Arthrobacter protophormiae endo-β-N-acetylglucosaminidase reveals a (β/α)8 catalytic domain, two ancillary domains and active site residues key for transglycosylation activity. J Mol Biol. 389:1-9.
    • (2009) J Mol Biol , vol.389 , pp. 1-9
    • Ling, Z.1    Suits, M.D.2    Bingham, R.J.3    Bruce, N.C.4    Davies, G.J.5    Fairbanks, A.J.6    Moir, J.W.7    Taylor, E.J.8
  • 19
    • 0028827570 scopus 로고
    • Endoplasmic reticulum-to-cytosol transport of free polymannose oligosaccharides in permeabilized HepG2 cells
    • Moore SE, Bauvy C, Codogno P. 1995. Endoplasmic reticulum-to-cytosol transport of free polymannose oligosaccharides in permeabilized HepG2 cells. EMBO J. 14:6034-6042.
    • (1995) EMBO J , vol.14 , pp. 6034-6042
    • Moore, S.E.1    Bauvy, C.2    Codogno, P.3
  • 20
    • 0034950461 scopus 로고    scopus 로고
    • Molecular cloning and expression of endo-β-N- acetylglucosaminidase D, which acts on the core structure of complex type asparagine-linked oligosaccharides
    • Muramatsu H, Tachikui H, Ushida H, Song X, Qiu Y, Yamamoto S, Muramatsu T. 2001. Molecular cloning and expression of endo-β-N- acetylglucosaminidase D, which acts on the core structure of complex type asparagine-linked oligosaccharides. J Biochem. 129:923-928.
    • (2001) J Biochem , vol.129 , pp. 923-928
    • Muramatsu, H.1    Tachikui, H.2    Ushida, H.3    Song, X.4    Qiu, Y.5    Yamamoto, S.6    Muramatsu, T.7
  • 21
    • 79959826593 scopus 로고    scopus 로고
    • The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG
    • Renzi F, Manfredi P, Mally M, Moes S, Jenö P, Cornelis GR. 2011. The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG. PLoS Pathog. 7: e1002118.
    • (2011) PLoS Pathog , vol.7
    • Renzi, F.1    Manfredi, P.2    Mally, M.3    Moes, S.4    Jenö, P.5    Cornelis, G.R.6
  • 22
    • 2442505584 scopus 로고    scopus 로고
    • Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation
    • Spiro RG. 2004. Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation. Cell Mol Life Sci. 61:1025-1041.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1025-1041
    • Spiro, R.G.1
  • 24
    • 84863711034 scopus 로고    scopus 로고
    • Free N-linked oligosaccharide chains: Formation and degradation
    • Suzuki T, Funakoshi Y. 2006. Free N-linked oligosaccharide chains: Formation and degradation. Glycoconj J. 23:291-302.
    • (2006) Glycoconj J , vol.23 , pp. 291-302
    • Suzuki, T.1    Funakoshi, Y.2
  • 25
    • 0032555648 scopus 로고    scopus 로고
    • Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity
    • Suzuki T, Park H, Kitajima K, Lennarz WJ. 1998. Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity. J Biol Chem. 273:21526-21530.
    • (1998) J Biol Chem , vol.273 , pp. 21526-21530
    • Suzuki, T.1    Park, H.2    Kitajima, K.3    Lennarz, W.J.4
  • 27
    • 0024377581 scopus 로고
    • Induction and purification of endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae grown in ovalbumin
    • Takegawa K, Nakoshi M, Iwahara S, Yamamoto K, Tochikura T. 1989. Induction and purification of endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae grown in ovalbumin. Appl Environ Microbiol. 55:3107-3112.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 3107-3112
    • Takegawa, K.1    Nakoshi, M.2    Iwahara, S.3    Yamamoto, K.4    Tochikura, T.5
  • 29
    • 0015954581 scopus 로고
    • Purification and properties of an endo-β-N-acetylglucosaminidase from Streptomyces griseus
    • Tarentino AL, Maley F. 1974. Purification and properties of an endo-β-N-acetylglucosaminidase from Streptomyces griseus. J Biol Chem. 249:811-817.
    • (1974) J Biol Chem , vol.249 , pp. 811-817
    • Tarentino, A.L.1    Maley, F.2
  • 30
    • 0026020091 scopus 로고
    • Identification of distinct endoglycosidase (endo) activities in Flavobacterium meningosepticum: Endo F1, endo F2, and endo F3. Endo F1 and endo H hydrolyze only high mannose and hybrid glycans
    • Trimble RB, Tarentino AL. 1991. Identification of distinct endoglycosidase (endo) activities in Flavobacterium meningosepticum: Endo F1, endo F2, and endo F3. Endo F1 and endo H hydrolyze only high mannose and hybrid glycans. J Biol Chem. 266:1646-1651.
    • (1991) J Biol Chem , vol.266 , pp. 1646-1651
    • Trimble, R.B.1    Tarentino, A.L.2
  • 31
    • 84865198114 scopus 로고    scopus 로고
    • Functional analysis of glycoside hydrolase family 18 and 20 genes in Neurospora crassa
    • Tzelepis GD, Melin P, Jensen DF, Stenlid J, Karlsson M. 2012. Functional analysis of glycoside hydrolase family 18 and 20 genes in Neurospora crassa. Fungal Genet Biol. 49:717-730.
    • (2012) Fungal Genet Biol , vol.49 , pp. 717-730
    • Tzelepis, G.D.1    Melin, P.2    Jensen, D.F.3    Stenlid, J.4    Karlsson, M.5
  • 32
    • 77956267399 scopus 로고    scopus 로고
    • Efficient transfer of sialo-oligosaccharide onto proteins by combined use of a glycosynthaselike mutant of Mucor hiemalis endoglycosidase and synthetic sialocomplex-type sugar oxazoline
    • Umekawa M, Higashiyama T, Koga Y, Tanaka T, Noguchi M, Kobayashi A, Shoda S, Huang W, Wang LX, Ashida H, et al. 2010. Efficient transfer of sialo-oligosaccharide onto proteins by combined use of a glycosynthaselike mutant of Mucor hiemalis endoglycosidase and synthetic sialocomplex-type sugar oxazoline. Biochim Biophys Acta. 1800:1203-1209.
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 1203-1209
    • Umekawa, M.1    Higashiyama, T.2    Koga, Y.3    Tanaka, T.4    Noguchi, M.5    Kobayashi, A.6    Shoda, S.7    Huang, W.8    Wang, L.X.9    Ashida, H.10
  • 33
    • 41949130819 scopus 로고    scopus 로고
    • Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities
    • Umekawa M, Huang W, Li B, Fujita K, Ashida H, Wang LX, Yamamoto K. 2008. Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities. J Biol Chem. 283:4469-4479.
    • (2008) J Biol Chem , vol.283 , pp. 4469-4479
    • Umekawa, M.1    Huang, W.2    Li, B.3    Fujita, K.4    Ashida, H.5    Wang, L.X.6    Yamamoto, K.7
  • 34
    • 73649089287 scopus 로고    scopus 로고
    • Efficient glycosynthase mutant derived from Mucor hiemalis endo-β-N-acetylglucosaminidase capable of transferring oligosaccharide from both sugar oxazoline and natural N-glycan
    • Umekawa M, Li C, Higashiyama T, Huang W, Ashida H, Yamamoto K, Wang LX. 2010. Efficient glycosynthase mutant derived from Mucor hiemalis endo-β-N-acetylglucosaminidase capable of transferring oligosaccharide from both sugar oxazoline and natural N-glycan. J Biol Chem. 285:511-521.
    • (2010) J Biol Chem , vol.285 , pp. 511-521
    • Umekawa, M.1    Li, C.2    Higashiyama, T.3    Huang, W.4    Ashida, H.5    Yamamoto, K.6    Wang, L.X.7
  • 36
    • 77949295782 scopus 로고    scopus 로고
    • Lectin-like ERAD players in ER and cytosol
    • Yoshida Y, Tanaka K. 2010. Lectin-like ERAD players in ER and cytosol. Biochim Biophys Acta. 1800:172-180.
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 172-180
    • Yoshida, Y.1    Tanaka, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.