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Volumn 386, Issue 2, 2005, Pages 395-400

Analysis of normal and mutant iduronate-2-sulphatase conformation

Author keywords

Heat denaturation; Iduronate 2 sulphatase (IDS); Mucopolysaccharidosis type II (MPS II); Mutant protein; Protein conformation

Indexed keywords

AMINO ACIDS; ANTIBODIES; CATALYSIS; CONFORMATIONS; POLYSACCHARIDES;

EID: 14844325339     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040739     Document Type: Article
Times cited : (14)

References (34)
  • 1
    • 0034987576 scopus 로고    scopus 로고
    • 1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family
    • Boltes, I., Czapinska, H., Kahnert, A., von Bulow, R., Dierks, T., Schmidt, B., von Figura, K., Kertesz, M. A. and Uson, I. (2001) 1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family. Structure 9, 483-491
    • (2001) Structure , vol.9 , pp. 483-491
    • Boltes, I.1    Czapinska, H.2    Kahnert, A.3    Von Bulow, R.4    Dierks, T.5    Schmidt, B.6    Von Figura, K.7    Kertesz, M.A.8    Uson, I.9
  • 3
    • 0032539976 scopus 로고    scopus 로고
    • Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis
    • Lukatela, G., Krauss, N., Theis, K., Selmer, T., Gieselmann, V., von Figura, K. and Saenger, W. (1998) Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry 37, 3654-3664
    • (1998) Biochemistry , vol.37 , pp. 3654-3664
    • Lukatela, G.1    Krauss, N.2    Theis, K.3    Selmer, T.4    Gieselmann, V.5    Von Figura, K.6    Saenger, W.7
  • 4
    • 0035847029 scopus 로고    scopus 로고
    • Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis
    • von Bulow, R., Schmidt, B., Dierks, T., von Figura, K. and Uson, I. (2001) Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis. J. Mol. Biol. 305, 269-277
    • (2001) J. Mol. Biol. , vol.305 , pp. 269-277
    • Von Bulow, R.1    Schmidt, B.2    Dierks, T.3    Von Figura, K.4    Uson, I.5
  • 5
    • 0029130352 scopus 로고
    • A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
    • Schmidt, B., Selmer, T., Ingendoh, A. and von Figura, K. (1995) A novel amino acid modification in sulfatases that is defective In multiple sulfatase deficiency. Cell (Cambridge, Mass.) 82, 271-278
    • (1995) Cell (Cambridge, Mass.) , vol.82 , pp. 271-278
    • Schmidt, B.1    Selmer, T.2    Ingendoh, A.3    Von Figura, K.4
  • 6
    • 0029898602 scopus 로고    scopus 로고
    • The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri
    • Selmer, T., Hallmann, A., Schmidt, B., Sumper, M. and von Figura, K. (1996) The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri. Eur. J. Biochem. 238, 341-345
    • (1996) Eur. J. Biochem. , vol.238 , pp. 341-345
    • Selmer, T.1    Hallmann, A.2    Schmidt, B.3    Sumper, M.4    Von Figura, K.5
  • 7
    • 0032570561 scopus 로고    scopus 로고
    • Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine
    • Miech, C., Dierks, T., Selmer, T., von Figura, K. and Schmidt, B. (1998) Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. J. Biol. Chem. 273, 4835-4837
    • (1998) J. Biol. Chem. , vol.273 , pp. 4835-4837
    • Miech, C.1    Dierks, T.2    Selmer, T.3    Von Figura, K.4    Schmidt, B.5
  • 8
    • 0032475864 scopus 로고    scopus 로고
    • Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine
    • Dierks, T., Miech, C., Hummerjohann, J., Schmidt, B., Kertesz, M. A. and von Figura, K. (1998) Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J. Biol. Chem. 273, 25560-25564
    • (1998) J. Biol. Chem. , vol.273 , pp. 25560-25564
    • Dierks, T.1    Miech, C.2    Hummerjohann, J.3    Schmidt, B.4    Kertesz, M.A.5    Von Figura, K.6
  • 10
    • 0032104543 scopus 로고    scopus 로고
    • A novel protein modification generating an aldehyde group in sulfatases: Its role in catalysis and disease
    • von Figura, K., Schmidt, B., Seimer, T. and Dierks, T. (1998) A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease. Bioessays 20, 505-510
    • (1998) Bioessays , vol.20 , pp. 505-510
    • Von Figura, K.1    Schmidt, B.2    Seimer, T.3    Dierks, T.4
  • 11
    • 0000869162 scopus 로고    scopus 로고
    • The mucopolysaccharidoses
    • (Scriver, C. R., Beaudet, A. L., Sly, W. S. and Valle, D., eds.), 8th edn, McGraw-Hill, New York
    • Neufeld, E. F. and Muenzer, J. (2001) The mucopolysaccharidoses. In The Metabolic and Molecular Bases of Inherited Diseases (Scriver, C. R., Beaudet, A. L., Sly, W. S. and Valle, D., eds.), 8th edn, pp. 3421-3452, McGraw-Hill, New York
    • (2001) The Metabolic and Molecular Bases of Inherited Diseases , pp. 3421-3452
    • Neufeld, E.F.1    Muenzer, J.2
  • 13
    • 0020355844 scopus 로고
    • Review: Genetics of steroid sulphatase deficiency and X-linked ichthyosis
    • Crawfurd, M. A. (1982) Review: genetics of steroid sulphatase deficiency and X-linked ichthyosis. J. Inherit. Metab. Dis. 5, 153-163
    • (1982) J. Inherit. Metab. Dis. , vol.5 , pp. 153-163
    • Crawfurd, M.A.1
  • 14
    • 0033166502 scopus 로고    scopus 로고
    • Processing of normal lysosomal and mutant N-acetylgalactosamine 4-sulphatase: BiP (immunoglobulin heavy-chain binding protein) may interact with critical protein contact sites
    • Bradford, T. M., Gething, M. J., Davey, R., Hopwood, J. J. and Brooks, D. A. (1999) Processing of normal lysosomal and mutant N-acetylgalactosamine 4-sulphatase: BiP (immunoglobulin heavy-chain binding protein) may interact with critical protein contact sites. Biochem. J. 341, 193-201
    • (1999) Biochem. J. , vol.341 , pp. 193-201
    • Bradford, T.M.1    Gething, M.J.2    Davey, R.3    Hopwood, J.J.4    Brooks, D.A.5
  • 15
    • 0037390834 scopus 로고    scopus 로고
    • Mutational spectrum of the iduronate 2 sulfatase gene in 25 unrelated Korean Hunter syndrome patients: Identification of 13 novel mutations
    • Kim, C. H., Hwang, H. Z., Song, S. M., Paik, K. H., Kwon, E. K., Moon, K. B., Yoon, J. H., Han, C. K. and Jin, D. K. (2003) Mutational spectrum of the iduronate 2 sulfatase gene in 25 unrelated Korean Hunter syndrome patients: identification of 13 novel mutations. Hum. Mutat. 21, 449-450
    • (2003) Hum. Mutat. , vol.21 , pp. 449-450
    • Kim, C.H.1    Hwang, H.Z.2    Song, S.M.3    Paik, K.H.4    Kwon, E.K.5    Moon, K.B.6    Yoon, J.H.7    Han, C.K.8    Jin, D.K.9
  • 17
    • 0023102699 scopus 로고
    • Hunter syndrome: Presence of material cross-reacting with antibodies against iduronate sulphatase
    • Daniele, A. and Di Natale, P. (1987) Hunter syndrome: presence of material cross-reacting with antibodies against iduronate sulphatase. Hum. Genet. 75, 234-238
    • (1987) Hum. Genet. , vol.75 , pp. 234-238
    • Daniele, A.1    Di Natale, P.2
  • 18
    • 0025047301 scopus 로고
    • Human liver iduronate-2-sulphatase: Purification, characterization and catalytic properties
    • Bielicki, J., Freeman, C., Clements, P. R. and Hopwood, J. J. (1990) Human liver iduronate-2-sulphatase: purification, characterization and catalytic properties. Biochem. J. 271, 75-86
    • (1990) Biochem. J. , vol.271 , pp. 75-86
    • Bielicki, J.1    Freeman, C.2    Clements, P.R.3    Hopwood, J.J.4
  • 19
    • 0029041456 scopus 로고
    • Processing of iduronate 2-sulphatase in human fibroblasts
    • Froissart, R., Millat, G., Mathieu, M., Bozon, D. and Maire, I. (1995) Processing of iduronate 2-sulphatase in human fibroblasts. Biochem. J. 309, 425-430
    • (1995) Biochem. J. , vol.309 , pp. 425-430
    • Froissart, R.1    Millat, G.2    Mathieu, M.3    Bozon, D.4    Maire, I.5
  • 20
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C., Braakman, I. and Helenius, A. (1994) Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. U.S.A. 91, 913-917
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 21
    • 0030928564 scopus 로고    scopus 로고
    • Characterization of iduronate sulphatase mutants affecting N-glycosylation sites and the cysteine-84 residue
    • Millat, G., Froissart, R., Maire, I. and Bozon, D. (1997) Characterization of iduronate sulphatase mutants affecting N-glycosylation sites and the cysteine-84 residue. Biochem. J. 326, 243-247
    • (1997) Biochem. J. , vol.326 , pp. 243-247
    • Millat, G.1    Froissart, R.2    Maire, I.3    Bozon, D.4
  • 22
    • 0020417388 scopus 로고
    • Multiple forms of iduronate 2-sulphate sulphatase in human tissues and body fluids
    • Archer, I. M., Harper, P. S. and Wusteman, F. S. (1982) Multiple forms of iduronate 2-sulphate sulphatase in human tissues and body fluids. Biochim. Biophys. Acta 708, 134-140
    • (1982) Biochim. Biophys. Acta , vol.708 , pp. 134-140
    • Archer, I.M.1    Harper, P.S.2    Wusteman, F.S.3
  • 23
    • 0346059410 scopus 로고    scopus 로고
    • Iduronate-2-sulphatase protein detection in plasma from mucopolysaccharidosis type II patients
    • Parkinson, E. J., Muller, V., Hopwood, J. J. and Brooks, D. A. (2004) Iduronate-2-sulphatase protein detection in plasma from mucopolysaccharidosis type II patients. Mol. Genet. Metab. 81, 58-64
    • (2004) Mol. Genet. Metab. , vol.81 , pp. 58-64
    • Parkinson, E.J.1    Muller, V.2    Hopwood, J.J.3    Brooks, D.A.4
  • 24
    • 0029113319 scopus 로고
    • Conformational changes in mutant lysozymes detected with monoclonal antibody
    • Kato, A., Shimizu, T. and Saga, S. (1995) Conformational changes in mutant lysozymes detected with monoclonal antibody. FEBS Lett. 371, 17-20
    • (1995) FEBS Lett. , vol.371 , pp. 17-20
    • Kato, A.1    Shimizu, T.2    Saga, S.3
  • 25
    • 0032847543 scopus 로고    scopus 로고
    • Monoclonal antibodies specific for the native, disease-associated isoform of the prion protein
    • Korth, C., Streit, P. and Oesch, B. (1999) Monoclonal antibodies specific for the native, disease-associated isoform of the prion protein. Methods Enzymol. 309, 106-122
    • (1999) Methods Enzymol. , vol.309 , pp. 106-122
    • Korth, C.1    Streit, P.2    Oesch, B.3
  • 26
    • 0037438317 scopus 로고    scopus 로고
    • Monoclonal antibodies as a probe for the unfolding of porcine growth hormone
    • Borromeo, V., Gaggioli, D., Berrini, A. and Secchi, C. (2003) Monoclonal antibodies as a probe for the unfolding of porcine growth hormone. J. Immunol. Methods 272, 107-115
    • (2003) J. Immunol. Methods , vol.272 , pp. 107-115
    • Borromeo, V.1    Gaggioli, D.2    Berrini, A.3    Secchi, C.4
  • 27
    • 0025779840 scopus 로고
    • Analysis of N-acetylgalactosamine-4-sulfatase protein and kinetics in mucopolysaccharidosis type VI patients
    • Brooks, D. A., McCourt, P. A., Gibson, G. J., Ashton, L. J., Shutter, M. and Hopwood, J. J. (1991) Analysis of N-acetylgalactosamine-4-sulfatase protein and kinetics in mucopolysaccharidosis type VI patients. Am. J. Hum. Genet. 48, 710-719
    • (1991) Am. J. Hum. Genet. , vol.48 , pp. 710-719
    • Brooks, D.A.1    McCourt, P.A.2    Gibson, G.J.3    Ashton, L.J.4    Shutter, M.5    Hopwood, J.J.6
  • 28
    • 0027402648 scopus 로고
    • Recombinant human iduronate-2-sulphatase: Correction of mucopolysaccharidosis-type II fibroblasts and characterization of the purified enzyme
    • Bielicki, J., Hopwood, J. J., Wilson, P. J. and Anson, D. S. (1993) Recombinant human iduronate-2-sulphatase: correction of mucopolysaccharidosis- type II fibroblasts and characterization of the purified enzyme. Biochem. J. 289, 241-246
    • (1993) Biochem. J. , vol.289 , pp. 241-246
    • Bielicki, J.1    Hopwood, J.J.2    Wilson, P.J.3    Anson, D.S.4
  • 29
    • 0032775996 scopus 로고    scopus 로고
    • Immune response to enzyme replacement therapy: 4-sulfatase epitope reactivity of plasma antibodies from MPS VI cats
    • Turner, C. T., Hopwood, J. J., Bond, C. S. and Brooks, D. A. (1999) Immune response to enzyme replacement therapy: 4-sulfatase epitope reactivity of plasma antibodies from MPS VI cats. Mol. Genet. Metab. 67, 194-205
    • (1999) Mol. Genet. Metab. , vol.67 , pp. 194-205
    • Turner, C.T.1    Hopwood, J.J.2    Bond, C.S.3    Brooks, D.A.4
  • 30
    • 0037906571 scopus 로고    scopus 로고
    • Immune tolerance after long-term enzyme-replacement therapy among patients who have mucopolysaccharidosis I
    • Kakavanos, R., Turner, C. T., Hopwood, J. J., Kakkis, E. D. and Brooks, D. A. (2003) Immune tolerance after long-term enzyme-replacement therapy among patients who have mucopolysaccharidosis I. Lancet 361, 1608-1613
    • (2003) Lancet , vol.361 , pp. 1608-1613
    • Kakavanos, R.1    Turner, C.T.2    Hopwood, J.J.3    Kakkis, E.D.4    Brooks, D.A.5
  • 32
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 33
    • 0035576329 scopus 로고    scopus 로고
    • Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes
    • Galperin, M. Y. and Jedrzejas, M. J. (2001) Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes. Proteins 45, 318-324
    • (2001) Proteins , vol.45 , pp. 318-324
    • Galperin, M.Y.1    Jedrzejas, M.J.2
  • 34
    • 17544373725 scopus 로고    scopus 로고
    • Structural analysis of bovine somatotropin using monoclonal antibodies and the conformation-sensitive immunoassay
    • Pfund, W. P., Bourdage, J. S. and Farley, K. A. (1996) Structural analysis of bovine somatotropin using monoclonal antibodies and the conformation-sensitive immunoassay. J. Biol. Chem. 271, 14055-14061
    • (1996) J. Biol. Chem. , vol.271 , pp. 14055-14061
    • Pfund, W.P.1    Bourdage, J.S.2    Farley, K.A.3


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