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Volumn 9, Issue 11, 2013, Pages 739-745

Insights into mucopolysaccharidosis I from the structure and action of α-L-iduronidase

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; FIBRONECTIN; IDURONIC ACID; LEVO IDURONIDASE;

EID: 84886594873     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1357     Document Type: Article
Times cited : (48)

References (50)
  • 1
    • 38949143787 scopus 로고    scopus 로고
    • The mucopolysaccharidoses: A success of molecular medicine
    • Clarke, L.A. The mucopolysaccharidoses: A success of molecular medicine. Expert Rev. Mol. Med. 10, e1 (2008).
    • (2008) Expert Rev. Mol. Med. , vol.10
    • Clarke, L.A.1
  • 2
    • 0021998174 scopus 로고
    • The clinical spectrum of a-l-iduronidase deficiency
    • Roubicek, M., Gehler, J. & Spranger, J. The clinical spectrum of a-l-iduronidase deficiency. Am. J. Med. Genet. 20, 471-481 (1985).
    • (1985) Am. J. Med. Genet. , vol.20 , pp. 471-481
    • Roubicek, M.1    Gehler, J.2    Spranger, J.3
  • 3
    • 79957628617 scopus 로고    scopus 로고
    • Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders
    • Valenzano, K.J. et al. Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders. Assay Drug Dev. Technol. 9, 213-235 (2011).
    • (2011) Assay Drug Dev. Technol. , vol.9 , pp. 213-235
    • Valenzano, K.J.1
  • 4
    • 59449109683 scopus 로고    scopus 로고
    • Identification of pharmacological chaperones for Gaucher disease and characterization of their effects on b-glucocerebrosidase by hydrogen/deuterium exchange mass spectrometry
    • Tropak, M.B. et al. Identification of pharmacological chaperones for Gaucher disease and characterization of their effects on b-glucocerebrosidase by hydrogen/deuterium exchange mass spectrometry. ChemBioChem 9, 2650-2662 (2008).
    • (2008) ChemBioChem , vol.9 , pp. 2650-2662
    • Tropak, M.B.1
  • 5
    • 34748914170 scopus 로고    scopus 로고
    • Pharmacologic chaperoning as a strategy to treat Gaucher disease
    • Yu, Z., Sawkar, A.R. & Kelly, J.W. Pharmacologic chaperoning as a strategy to treat Gaucher disease. FEBS J. 274, 4944-4950 (2007).
    • (2007) FEBS J , vol.274 , pp. 4944-4950
    • Yu, Z.1    Sawkar, A.R.2    Kelly, J.W.3
  • 7
    • 0041524060 scopus 로고    scopus 로고
    • Can mucopolysaccharidosis type I disease severity be predicted based on a patient's genotype? A comprehensive review of the literature
    • Terlato, N.J. & Cox, G.F. Can mucopolysaccharidosis type I disease severity be predicted based on a patient's genotype? A comprehensive review of the literature. Genet. Med. 5, 286-294 (2003).
    • (2003) Genet. Med. , vol.5 , pp. 286-294
    • Terlato, N.J.1    Cox, G.F.2
  • 8
    • 0037709362 scopus 로고    scopus 로고
    • Family 39 a-l-iduronidases and b-d-xylosidases react through similar glycosyl-enzyme intermediates: Identification of the human iduronidase nucleophile
    • Nieman, C.E. et al. Family 39 a-l-iduronidases and b-d-xylosidases react through similar glycosyl-enzyme intermediates: Identification of the human iduronidase nucleophile. Biochemistry 42, 8054-8065 (2003).
    • (2003) Biochemistry , vol.42 , pp. 8054-8065
    • Nieman, C.E.1
  • 9
    • 10744221210 scopus 로고    scopus 로고
    • Crystal structure of b-d-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase
    • Yang, J.K. et al. Crystal structure of b-d-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase. J. Mol. Biol. 335, 155-165 (2004).
    • (2004) J. Mol. Biol. , vol.335 , pp. 155-165
    • Yang, J.K.1
  • 11
    • 18044399158 scopus 로고    scopus 로고
    • A homology model for human a-liduronidase: Insights into human disease
    • Rempel, B.P., Clarke, L.A. & Withers, S.G. A homology model for human a-liduronidase: Insights into human disease. Mol. Genet. Metab. 85, 28-37 (2005).
    • (2005) Mol. Genet. Metab. , vol.85 , pp. 28-37
    • Rempel, B.P.1    Clarke, L.A.2    Withers, S.G.3
  • 12
    • 0030954670 scopus 로고    scopus 로고
    • Carbohydrate structures of recombinant human a-l-iduronidase secreted by Chinese hamster ovary cells
    • Zhao, K.W., Faull, K.F., Kakkis, E.D. & Neufeld, E.F. Carbohydrate structures of recombinant human a-l-iduronidase secreted by Chinese hamster ovary cells. J. Biol. Chem. 272, 22758-22765 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 22758-22765
    • Zhao, K.W.1    Faull, K.F.2    Kakkis, E.D.3    Neufeld, E.F.4
  • 13
    • 84888136369 scopus 로고    scopus 로고
    • Characterization and downstream mannose phosphorylation of human recombinant alpha-L-iduronidase produced in Arabidopsis complex glycan-deficient (cgl) seeds
    • doi:10.1111/pbi.12096 (31 July 2013
    • He, X. et al. Characterization and downstream mannose phosphorylation of human recombinant alpha-L-iduronidase produced in Arabidopsis complex glycan-deficient (cgl) seeds. Plant Biotechnol J. doi:10.1111/pbi.12096 (31 July 2013).
    • Plant Biotechnol J.
    • He, X.1
  • 14
    • 0032532593 scopus 로고    scopus 로고
    • Identification of glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum b-xylosidase using electrospray MS
    • Vocadlo, D.J., MacKenzie, L.F., He, S., Zeikus, G.J. & Withers, S.G. Identification of glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum b-xylosidase using electrospray MS. Biochem. J. 335, 449-455 (1998).
    • (1998) Biochem. J. , vol.335 , pp. 449-455
    • Vocadlo, D.J.1    MacKenzie, L.F.2    He, S.3    Zeikus, G.J.4    Withers, S.G.5
  • 15
    • 0029876033 scopus 로고    scopus 로고
    • Stereochemical course and reaction products of the action of b-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI
    • Armand, S. et al. Stereochemical course and reaction products of the action of b-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI. Eur. J. Biochem. 236, 706-713 (1996).
    • (1996) Eur. J. Biochem. , vol.236 , pp. 706-713
    • Armand, S.1
  • 16
    • 79251535315 scopus 로고    scopus 로고
    • Graphical analysis of pH-dependent properties of proteins predicted using PROPKA. BMC
    • Rostkowski, M., Olsson, M.H., Sondergaard, C.R. & Jensen, J.H. Graphical analysis of pH-dependent properties of proteins predicted using PROPKA. BMC Struct. Biol. 11, 6 (2011).
    • (2011) Struct. Biol. , vol.11 , Issue.6
    • Rostkowski, M.1    Olsson, M.H.2    Sondergaard, C.R.3    Jensen, J.H.4
  • 17
    • 84883376707 scopus 로고    scopus 로고
    • Human a-l-iduronidase uses its own N-glycan as a substratebinding and catalytic module
    • Maita, N. et al. Human a-l-iduronidase uses its own N-glycan as a substratebinding and catalytic module. Proc. Natl. Acad. Sci. USA 110, 14628-14633 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 14628-14633
    • Maita, N.1
  • 18
    • 0020067351 scopus 로고
    • Diagnostic enzymology of a-l-iduronidase with special reference to a sulfated disaccharide derived from heparin
    • Hopwood, J.J. & Muller, V. Diagnostic enzymology of a-l-iduronidase with special reference to a sulfated disaccharide derived from heparin. Clin. Sci. (Lond.) 62, 193-201 (1982).
    • (1982) Clin. Sci. (Lond.) , vol.62 , pp. 193-201
    • Hopwood, J.J.1    Muller, V.2
  • 19
    • 4143144349 scopus 로고    scopus 로고
    • Identification and molecular characterization of a-liduronidase mutations present in mucopolysaccharidosis type I patients undergoing enzyme replacement therapy
    • Yogalingam, G. et al. Identification and molecular characterization of a-liduronidase mutations present in mucopolysaccharidosis type I patients undergoing enzyme replacement therapy. Hum. Mutat. 24, 199-207 (2004).
    • (2004) Hum. Mutat. , vol.24 , pp. 199-207
    • Yogalingam, G.1
  • 20
    • 0022242361 scopus 로고
    • Human a-l-iduronidase. 2. Catalytic properties
    • Clements, P.R., Muller, V. & Hopwood, J.J. Human a-l-iduronidase. 2. Catalytic properties. Eur. J. Biochem. 152, 29-34 (1985).
    • (1985) Eur. J. Biochem. , vol.152 , pp. 29-34
    • Clements, P.R.1    Muller, V.2    Hopwood, J.J.3
  • 21
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • Vocadlo, D.J., Davies, G.J., Laine, R. & Withers, S.G. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412, 835-838 (2001).
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 22
    • 84860298921 scopus 로고    scopus 로고
    • Conformational analyses of the reaction coordinate of glycosidases
    • Davies, G.J., Planas, A. & Rovira, C. Conformational analyses of the reaction coordinate of glycosidases. Acc. Chem. Res. 45, 308-316 (2012).
    • (2012) Acc. Chem. Res. , vol.45 , pp. 308-316
    • Davies, G.J.1    Planas, A.2    Rovira, C.3
  • 23
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland, D.E. Stereochemistry and the mechanism of enzymatic reactions. Biol. Rev. Camb. Philos. Soc. 28, 416-436 (1953).
    • (1953) Biol. Rev. Camb. Philos. Soc. , vol.28 , pp. 416-436
    • Koshland, D.E.1
  • 24
    • 0033559148 scopus 로고    scopus 로고
    • Recent insights into inhibition, structure, and mechanism of configuration-retaining glycosidases
    • Heightman, T.D. & Vasella, A.T. Recent insights into inhibition, structure, and mechanism of configuration-retaining glycosidases. Angew. Chem. Int. Edn Engl. 38, 750-770 (1999).
    • (1999) Angew. Chem. Int. Edn Engl. , vol.38 , pp. 750-770
    • Heightman, T.D.1    Vasella, A.T.2
  • 25
    • 0033169002 scopus 로고    scopus 로고
    • Catalysis and specificity in enzymatic glycoside hydrolysis: A 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase
    • Sabini, E. et al. Catalysis and specificity in enzymatic glycoside hydrolysis: A 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase. Chem. Biol. 6, 483-492 (1999).
    • (1999) Chem. Biol. , vol.6 , pp. 483-492
    • Sabini, E.1
  • 26
    • 0033609135 scopus 로고    scopus 로고
    • Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase
    • Sidhu, G. et al. Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase. Biochemistry 38, 5346-5354 (1999).
    • (1999) Biochemistry , vol.38 , pp. 5346-5354
    • Sidhu, G.1
  • 27
    • 0347297299 scopus 로고    scopus 로고
    • Identification and characterization of 13 new mutations in mucopolysaccharidosis type I patients
    • Matte, U. et al. Identification and characterization of 13 new mutations in mucopolysaccharidosis type I patients. Mol. Genet. Metab. 78, 37-43 (2003).
    • (2003) Mol. Genet. Metab. , vol.78 , pp. 37-43
    • Matte, U.1
  • 28
    • 0032766994 scopus 로고    scopus 로고
    • Mucopolysaccharidosis type I: Characterization of a common mutation that causes Hurler syndrome in Moroccan subjects
    • Alif, N. et al. Mucopolysaccharidosis type I: Characterization of a common mutation that causes Hurler syndrome in Moroccan subjects. Ann. Hum. Genet. 63, 9-16 (1999).
    • (1999) Ann. Hum. Genet. , vol.63 , pp. 9-16
    • Alif, N.1
  • 29
    • 31644450230 scopus 로고    scopus 로고
    • Mucopolysaccharidosis I: A-l-iduronidase mutations in three Tunisian families
    • Laradi, S. et al. Mucopolysaccharidosis I: A-l-iduronidase mutations in three Tunisian families. J. Inherit. Metab. Dis. 28, 1019-1026 (2005).
    • (2005) J. Inherit. Metab. Dis. , vol.28 , pp. 1019-1026
    • Laradi, S.1
  • 30
    • 0027018480 scopus 로고
    • A-l-Iduronidase mutations (Q70X and P533R) associate with a severe Hurler phenotype
    • Scott, H.S. et al. a-l-Iduronidase mutations (Q70X and P533R) associate with a severe Hurler phenotype. Hum. Mutat. 1, 333-339 (1992).
    • (1992) Hum. Mutat. , vol.1 , pp. 333-339
    • Scott, H.S.1
  • 31
    • 0032413781 scopus 로고    scopus 로고
    • Genotype-phenotype correlations in mucopolysaccharidosis type I using enzyme kinetics, immunoquantification and in vitro turnover studies
    • Bunge, S. et al. Genotype-phenotype correlations in mucopolysaccharidosis type I using enzyme kinetics, immunoquantification and in vitro turnover studies. Biochim. Biophys. Acta 1407, 249-256 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1407 , pp. 249-256
    • Bunge, S.1
  • 32
    • 0001724322 scopus 로고
    • The synthesis of polyhydroxylated amino acids from glucuronolactone: Enantiospecific synthesis of 2S,3R,4R,5S-Trihydroxypipecolic acid, 2R,3R,4R,5S-Trihydroxypipecolic acid and 2R,3R,4R-dihydroxyproline
    • Bashyal, B.P., Chow, H.-F., Fellows, L.E. & Fleet, G.W.J. The synthesis of polyhydroxylated amino acids from glucuronolactone: Enantiospecific synthesis of 2S,3R,4R,5S-Trihydroxypipecolic acid, 2R,3R,4R,5S- Trihydroxypipecolic acid and 2R,3R,4R-dihydroxyproline. Tetrahedron 43, 415-422 (1987).
    • (1987) Tetrahedron , vol.43 , pp. 415-422
    • Bashyal, B.P.1    Chow, H.-F.2    Fellows, L.E.3    Fleet, G.W.J.4
  • 33
    • 33645112692 scopus 로고    scopus 로고
    • Synthesis of enzymatically active human á-l-iduronidase in Arabidopsis cgl (complex glycan-deficient) seeds
    • Downing, W.L. et al. Synthesis of enzymatically active human á-l-iduronidase in Arabidopsis cgl (complex glycan-deficient) seeds. Plant Biotechnol. J. 4, 169-181 (2006).
    • (2006) Plant Biotechnol. J. , vol.4 , pp. 169-181
    • Downing, W.L.1
  • 34
    • 84867016864 scopus 로고    scopus 로고
    • Production of á-l-iduronidase in maize for the potential treatment of a human lysosomal storage disease
    • He, X. et al. Production of á-l-iduronidase in maize for the potential treatment of a human lysosomal storage disease. Nat. Commun. 3, 1062 (2012).
    • (2012) Nat. Commun. , vol.3 , Issue.1062
    • He, X.1
  • 35
    • 84863416061 scopus 로고    scopus 로고
    • Influence of an ER-retention signal on the N-glycosylation of recombinant human á-l-iduronidase generated in seeds of Arabidopsis
    • He, X. et al. Influence of an ER-retention signal on the N-glycosylation of recombinant human á-l-iduronidase generated in seeds of Arabidopsis. Plant Mol. Biol. 79, 157-169 (2012).
    • (2012) Plant Mol. Biol. , vol.79 , pp. 157-169
    • He, X.1
  • 36
    • 0034096547 scopus 로고    scopus 로고
    • Á-l-iduronidase forms semi-crystalline spherulites with amyloid-like properties
    • Ruth, L., Eisenberg, D. & Neufeld, E.F. á-l-iduronidase forms semi-crystalline spherulites with amyloid-like properties. Acta Crystallogr. D Biol. Crystallogr. 56, 524-528 (2000).
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 524-528
    • Ruth, L.1    Eisenberg, D.2    Neufeld, E.F.3
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 76449098262 scopus 로고    scopus 로고
    • Phenix: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 40
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S.X., Lamzin, V.S. & Perrakis, A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3, 1171-1179 (2008).
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 42
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M.D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 43
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G.N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D Biol. Crystallogr. 67, 355-367 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 44
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word, J.M., Lovell, S.C., Richardson, J.S. & Richardson, D.C. Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation. J. Mol. Biol. 285, 1735-1747 (1999).
    • (1999) J. Mol. Biol. , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 45
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 46
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn, M.D., Murshudov, G.N. & Papiz, M.Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374, 300-321 (2003).
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 47
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J. & Merritt, E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 48
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., Macarthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 49
    • 34250669555 scopus 로고    scopus 로고
    • Psite vectors for stable integration or transient expression of autofluorescent protein fusions in plants: Probing Nicotiana benthamiana-virus interactions
    • Chakrabarty, R. et al. PSITE vectors for stable integration or transient expression of autofluorescent protein fusions in plants: Probing Nicotiana benthamiana-virus interactions. Mol. Plant Microbe Interact. 20, 740-750 (2007).
    • (2007) Mol. Plant Microbe Interact. , vol.20 , pp. 740-750
    • Chakrabarty, R.1
  • 50
    • 84862585334 scopus 로고    scopus 로고
    • Pharmacological chaperones facilitate the post-ER transport of recombinant N370S mutant â-glucocerebrosidase in plant cells: Evidence that N370S is a folding mutant
    • Babajani, G., Tropak, M.B., Mahuran, D.J. & Kermode, A.R. Pharmacological chaperones facilitate the post-ER transport of recombinant N370S mutant â-glucocerebrosidase in plant cells: Evidence that N370S is a folding mutant. Mol. Genet. Metab. 106, 323-329 (2012).
    • (2012) Mol. Genet. Metab. , vol.106 , pp. 323-329
    • Babajani, G.1    Tropak, M.B.2    Mahuran, D.J.3    Kermode, A.R.4


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