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Volumn 280, Issue 18, 2013, Pages 4560-4571

Structure of a bacterial glycoside hydrolase family 63 enzyme in complex with its glycosynthase product, and insights into the substrate specificity

Author keywords

( )6 barrel; collagen; glycoside hydrolase family 63; glycosynthase; processing glucosidase I

Indexed keywords

2 O ALPHA DEXTRO GLUCOPYRANOSYL ALPHA DEXTRO GALACTOPYRANOSE; DISACCHARIDE; GALACTOSE; GLUCOSE; GLYCOSIDASE; GLYCOSIDE HYDROLASE FAMILY 63; GLYCOSYNTHASE; MELIBIOSE; UNCLASSIFIED DRUG;

EID: 84883452283     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12424     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 0032714568 scopus 로고    scopus 로고
    • Importance of glycosidases in mammalian glycoprotein biosynthesis
    • Herscovics A, (1999) Importance of glycosidases in mammalian glycoprotein biosynthesis. Biochim Biophys Acta 1473, 96-107.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 96-107
    • Herscovics, A.1
  • 2
    • 0028213490 scopus 로고
    • Glycosidases of the asparagine-linked oligosaccharide processing pathway
    • Moremen KW, Trimble RB, &, Herscovics A, (1994) Glycosidases of the asparagine-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
  • 3
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A, &, Aebi M, (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73, 1019-1049.
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 4
    • 84863810208 scopus 로고    scopus 로고
    • Heterologous expression and characterization of processing α-glucosidase i from Aspergillus brasiliensis ATCC 9642
    • Miyazaki T, Matsumoto Y, Matsuda K, Kurakata Y, Matsuo I, Ito Y, Nishikawa A, &, Tonozuka T, (2011) Heterologous expression and characterization of processing α-glucosidase I from Aspergillus brasiliensis ATCC 9642. Glycoconj J 28, 563-571.
    • (2011) Glycoconj J , vol.28 , pp. 563-571
    • Miyazaki, T.1    Matsumoto, Y.2    Matsuda, K.3    Kurakata, Y.4    Matsuo, I.5    Ito, Y.6    Nishikawa, A.7    Tonozuka, T.8
  • 6
    • 0036259187 scopus 로고    scopus 로고
    • Overexpression, purification, and partial characterization of Saccharomyces cerevisiae processing alpha glucosidase i
    • Dhanawansa R, Faridmoayer A, van der Merwe G, Li YX, &, Scaman CH, (2002) Overexpression, purification, and partial characterization of Saccharomyces cerevisiae processing alpha glucosidase I. Glycobiology 12, 229-234.
    • (2002) Glycobiology , vol.12 , pp. 229-234
    • Dhanawansa, R.1    Faridmoayer, A.2    Van Der Merwe, G.3    Li, Y.X.4    Scaman, C.H.5
  • 7
    • 53249147141 scopus 로고    scopus 로고
    • Not just for Eukarya anymore: Protein glycosylation in Bacteria and Archaea
    • Abu-Qarn M, Eichler J, &, Sharon N, (2008) Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea. Curr Opin Struct Biol 18, 544-550.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 544-550
    • Abu-Qarn, M.1    Eichler, J.2    Sharon, N.3
  • 8
    • 46649103223 scopus 로고    scopus 로고
    • Structural insights into the substrate specificity and function of Escherichia coli K12 YgjK, a glucosidase belonging to the glycoside hydrolase family 63
    • Kurakata Y, Uechi A, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, &, Tonozuka T, (2008) Structural insights into the substrate specificity and function of Escherichia coli K12 YgjK, a glucosidase belonging to the glycoside hydrolase family 63. J Mol Biol 381, 116-128.
    • (2008) J Mol Biol , vol.381 , pp. 116-128
    • Kurakata, Y.1    Uechi, A.2    Yoshida, H.3    Kamitori, S.4    Sakano, Y.5    Nishikawa, A.6    Tonozuka, T.7
  • 11
    • 84877713668 scopus 로고    scopus 로고
    • Specificity of processing α-glucosidase i is guided by the substrate conformation: Crystallographic and in silico studies
    • Barker MK, &, Rose DR, (2013) Specificity of processing α-glucosidase I is guided by the substrate conformation: crystallographic and in silico studies. J Biol Chem 288, 13563-13574.
    • (2013) J Biol Chem , vol.288 , pp. 13563-13574
    • Barker, M.K.1    Rose, D.R.2
  • 13
    • 0026726797 scopus 로고
    • Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2 Å resolution
    • Aleshin A, Golubev A, Firsov LM, &, Honzatko RB, (1992) Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2 Å resolution. J Biol Chem 267, 19291-19298.
    • (1992) J Biol Chem , vol.267 , pp. 19291-19298
    • Aleshin, A.1    Golubev, A.2    Firsov, L.M.3    Honzatko, R.B.4
  • 14
    • 33646236579 scopus 로고    scopus 로고
    • Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain
    • Ševcík J, Hostinová E, Solovicová A, Gasperík J, Dauter Z, &, Wilson KS, (2006) Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain. FEBS J 273, 2161-2171.
    • (2006) FEBS J , vol.273 , pp. 2161-2171
    • Ševcík, J.1    Hostinová, E.2    Solovicová, A.3    Gasperík, J.4    Dauter, Z.5    Wilson, K.S.6
  • 16
    • 0034885657 scopus 로고    scopus 로고
    • Crystal structure of maltose phosphorylase from Lactobacillus brevis: Unexpected evolutionary relationship with glucoamylases
    • Egloff MP, Uppenberg J, Haalck L, &, van Tilbeurgh H, (2001) Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases. Structure 9, 689-697.
    • (2001) Structure , vol.9 , pp. 689-697
    • Egloff, M.P.1    Uppenberg, J.2    Haalck, L.3    Van Tilbeurgh, H.4
  • 17
    • 79955427274 scopus 로고    scopus 로고
    • Analysis of a new family of widely distributed metal-independent α-mannosidases provides unique insight into the processing of N-linked glycans
    • Gregg KJ, Zandberg WF, Hehemann JH, Whitworth GE, Deng L, Vocadlo DJ, &, Boraston AB, (2011) Analysis of a new family of widely distributed metal-independent α-mannosidases provides unique insight into the processing of N-linked glycans. J Biol Chem 286, 15586-15596.
    • (2011) J Biol Chem , vol.286 , pp. 15586-15596
    • Gregg, K.J.1    Zandberg, W.F.2    Hehemann, J.H.3    Whitworth, G.E.4    Deng, L.5    Vocadlo, D.J.6    Boraston, A.B.7
  • 18
    • 33644983451 scopus 로고    scopus 로고
    • The first glycosynthase derived from an inverting glycoside hydrolase
    • Honda Y, &, Kitaoka M, (2006) The first glycosynthase derived from an inverting glycoside hydrolase. J Biol Chem 281, 1426-1431.
    • (2006) J Biol Chem , vol.281 , pp. 1426-1431
    • Honda, Y.1    Kitaoka, M.2
  • 21
    • 84862155984 scopus 로고    scopus 로고
    • A glycosynthase derived from an inverting GH19 chitinase from the moss Bryum coronatum
    • Ohnuma T, Fukuda T, Dozen S, Honda Y, Kitaoka M, &, Fukamizo T, (2012) A glycosynthase derived from an inverting GH19 chitinase from the moss Bryum coronatum. Biochem J 444, 437-443.
    • (2012) Biochem J , vol.444 , pp. 437-443
    • Ohnuma, T.1    Fukuda, T.2    Dozen, S.3    Honda, Y.4    Kitaoka, M.5    Fukamizo, T.6
  • 22
    • 0032503519 scopus 로고    scopus 로고
    • Glycosynthases: Mutant glycosidases for oligosaccharide synthesis
    • Mackenzie LF, Wang Q, Warren RAJ, &, Withers SG, (1998) Glycosynthases: mutant glycosidases for oligosaccharide synthesis. J Am Chem Soc 120, 5883-5884.
    • (1998) J Am Chem Soc , vol.120 , pp. 5883-5884
    • Mackenzie, L.F.1    Wang, Q.2    Warren, R.A.J.3    Withers, S.G.4
  • 23
    • 0036015487 scopus 로고    scopus 로고
    • Glycosynthases: New tools for oligosaccharide synthesis
    • Jakeman DL, &, Withers SG, (2002) Glycosynthases: new tools for oligosaccharide synthesis. Trends Glycosci Glycotechnol 14, 13-25.
    • (2002) Trends Glycosci Glycotechnol , vol.14 , pp. 13-25
    • Jakeman, D.L.1    Withers, S.G.2
  • 25
    • 65949085808 scopus 로고    scopus 로고
    • Conversion of inverting glycoside hydrolases into catalysts for synthesizing glycosides employing a glycosynthase strategy
    • Kitaoka M, Honda Y, Fushinobu S, Hidaka M, Katayama T, &, Yamamoto K, (2009) Conversion of inverting glycoside hydrolases into catalysts for synthesizing glycosides employing a glycosynthase strategy. Trends Glycosci Glycotechnol 21, 23-39.
    • (2009) Trends Glycosci Glycotechnol , vol.21 , pp. 23-39
    • Kitaoka, M.1    Honda, Y.2    Fushinobu, S.3    Hidaka, M.4    Katayama, T.5    Yamamoto, K.6
  • 26
    • 20444504291 scopus 로고    scopus 로고
    • Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125
    • Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shoun H, &, Kitaoka M, (2005) Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125. J Biol Chem 280, 17180-17186.
    • (2005) J Biol Chem , vol.280 , pp. 17180-17186
    • Fushinobu, S.1    Hidaka, M.2    Honda, Y.3    Wakagi, T.4    Shoun, H.5    Kitaoka, M.6
  • 27
    • 28444469149 scopus 로고    scopus 로고
    • Evolutionary and mechanistic relationships between glycosidases acting on α- And β-bonds
    • Stam MR, Blanc E, Coutinho PM, &, Henrissat B, (2005) Evolutionary and mechanistic relationships between glycosidases acting on α- and β-bonds. Carbohydr Res 340, 2728-2734.
    • (2005) Carbohydr Res , vol.340 , pp. 2728-2734
    • Stam, M.R.1    Blanc, E.2    Coutinho, P.M.3    Henrissat, B.4
  • 28
  • 29
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies GJ, Wilson KS, &, Henrissat B, (1997) Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J 321, 557-559.
    • (1997) Biochem J , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 30
    • 34447519035 scopus 로고    scopus 로고
    • The synthesis of 2-, 3-, 4- and 6-O-α- d -glucopyranosyl- d -galactopyranose, and their evaluation as nutritional supplements for pre-term infants
    • Meloncelli PJ, Williams TM, Hartmann PE, &, Stick RV, (2007) The synthesis of 2-, 3-, 4- and 6-O-α- d -glucopyranosyl- d -galactopyranose, and their evaluation as nutritional supplements for pre-term infants. Carbohydr Res 342, 1793-1804.
    • (2007) Carbohydr Res , vol.342 , pp. 1793-1804
    • Meloncelli, P.J.1    Williams, T.M.2    Hartmann, P.E.3    Stick, R.V.4
  • 31
    • 0028357194 scopus 로고
    • Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4 Å resolution
    • Aleshin AE, Firsov LM, &, Honzatko RB, (1994) Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4 Å resolution. J Biol Chem 269, 15631-15639.
    • (1994) J Biol Chem , vol.269 , pp. 15631-15639
    • Aleshin, A.E.1    Firsov, L.M.2    Honzatko, R.B.3
  • 32
    • 0027400361 scopus 로고
    • Functional roles of the invariant aspartic acid 55, tyrosine 306, and aspartic acid 309 in glucoamylase from Aspergillus awamori studied by mutagenesis
    • Sierks MR, &, Svensson B, (1993) Functional roles of the invariant aspartic acid 55, tyrosine 306, and aspartic acid 309 in glucoamylase from Aspergillus awamori studied by mutagenesis. Biochemistry 32, 1113-1117.
    • (1993) Biochemistry , vol.32 , pp. 1113-1117
    • Sierks, M.R.1    Svensson, B.2
  • 33
    • 0011720368 scopus 로고
    • Construction and characterization of mutant glucoamylases from the yeast Saccharomycopsis fibuligera
    • Itoh T, Sakata Y, Akada R, Nimi O, &, Yamashita I, (1989) Construction and characterization of mutant glucoamylases from the yeast Saccharomycopsis fibuligera. Agric Biol Chem 53, 3159-3167.
    • (1989) Agric Biol Chem , vol.53 , pp. 3159-3167
    • Itoh, T.1    Sakata, Y.2    Akada, R.3    Nimi, O.4    Yamashita, I.5
  • 34
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward S, &, Berendsen HJ, (1998) Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 30, 144-154.
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 35
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project.
    • Collaborative Computational Project (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 36
    • 0014217149 scopus 로고
    • The structure of the disaccharide unit of the renal glomerular basement membrane
    • Spiro RG, (1967) The structure of the disaccharide unit of the renal glomerular basement membrane. J Biol Chem 242, 4813-4823.
    • (1967) J Biol Chem , vol.242 , pp. 4813-4823
    • Spiro, R.G.1
  • 37
    • 0014690194 scopus 로고
    • Characterization and quantitative determination of the hydroxylysine-linked carbohydrate units of several collagens
    • Spiro RG, (1969) Characterization and quantitative determination of the hydroxylysine-linked carbohydrate units of several collagens. J Biol Chem 244, 602-612.
    • (1969) J Biol Chem , vol.244 , pp. 602-612
    • Spiro, R.G.1
  • 38
    • 0029873776 scopus 로고    scopus 로고
    • Improved rapid method for the isolation, purification and identification of collagen glycosides
    • Garza H, Bennett N Jr, &, Rodriguez GP, (1996) Improved rapid method for the isolation, purification and identification of collagen glycosides. J Chromatogr A 732, 385-389.
    • (1996) J Chromatogr A , vol.732 , pp. 385-389
    • Garza, H.1    Bennett, Jr.N.2    Rodriguez, G.P.3
  • 39
    • 84871684186 scopus 로고    scopus 로고
    • A new bacterial hydrolase specific for the compatible solutes α- D -mannopyranosyl-(1→2)- d -glycerate and α- D -glucopyranosyl- (1→2)- d -glycerate
    • Alarico S, Empadinhas N, &, da Costa MS, (2013) A new bacterial hydrolase specific for the compatible solutes α- d -mannopyranosyl- (1→2)- d -glycerate and α- d -glucopyranosyl-(1→2)- d -glycerate. Enzyme Microb Technol 52, 77-83.
    • (2013) Enzyme Microb Technol , vol.52 , pp. 77-83
    • Alarico, S.1    Empadinhas, N.2    Da Costa, M.S.3
  • 40
    • 0002763232 scopus 로고
    • Studies of specifically fluorinated carbohydrates. Part I. Nuclear magnetic resonance studies of hexopyranosyl fluoride derivatives
    • Hall LD, Manville JF, &, Bhacca NS, (1969) Studies of specifically fluorinated carbohydrates. Part I. Nuclear magnetic resonance studies of hexopyranosyl fluoride derivatives. Can J Chem 47, 1-17.
    • (1969) Can J Chem , vol.47 , pp. 1-17
    • Hall, L.D.1    Manville, J.F.2    Bhacca, N.S.3
  • 42
    • 16644392062 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of Escherichia coli K12 YgjK protein, a member of glycosyl hydrolase family 63
    • Tonozuka T, Uechi A, Mizuno M, Ichikawa K, Nishikawa A, &, Sakano Y, (2004) Crystallization and preliminary X-ray analysis of Escherichia coli K12 YgjK protein, a member of glycosyl hydrolase family 63. Acta Crystallogr D Biol Crystallogr 60, 1284-1285.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1284-1285
    • Tonozuka, T.1    Uechi, A.2    Mizuno, M.3    Ichikawa, K.4    Nishikawa, A.5    Sakano, Y.6
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, &, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, &, Teplyakov A, (1997) MOLREP: an automated program for molecular replacement. J Appl Crystallogr 30, 1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 47
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, &, Lamzin VS, (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6, 458-463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3


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