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Volumn 25, Issue 11, 2016, Pages 2234-2244

Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; ENZYME VARIANT; GALACTOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; GLUCOSE 1 PHOSPHATE; HOMODIMER; RECOMBINANT ENZYME; ZINC; GALACTOSE; TERNARY COMPLEX FACTOR;

EID: 84998879845     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddw091     Document Type: Article
Times cited : (39)

References (62)
  • 1
    • 0242498430 scopus 로고    scopus 로고
    • Structure and function of enzymes of the Leloir pathway for galactose metabolism
    • Holden, H.M., Rayment, I. and Thoden, J.B. (2003) Structure and function of enzymes of the Leloir pathway for galactose metabolism. J. Biol. Chem., 278, 43885-43888.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43885-43888
    • Holden, H.M.1    Rayment, I.2    Thoden, J.B.3
  • 2
    • 0029920614 scopus 로고    scopus 로고
    • The Leloir pathway: A mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose
    • Frey, P. (1996) the Leloir pathway: a mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose. Faseb J., 10, 461-470.
    • (1996) Faseb J. , vol.10 , pp. 461-470
    • Frey, P.1
  • 3
    • 33745830480 scopus 로고    scopus 로고
    • Glycogen branches out: New perspectives on the role of glycogen metabolism in the integration of metabolic pathways
    • Greenberg, C.C., Jurczak, M.J., Danos, A.M. and Brady, M.J. (2006) Glycogen branches out: new perspectives on the role of glycogen metabolism in the integration of metabolic pathways. Am. J. Physiol. Endocrinol. Metab., 291, 1-8.
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.291 , pp. 1-8
    • Greenberg, C.C.1    Jurczak, M.J.2    Danos, A.M.3    Brady, M.J.4
  • 4
    • 33746976801 scopus 로고    scopus 로고
    • Recent developments in glycoconjugates
    • Davis, B. (1999) Recent developments in glycoconjugates. J. Chem. Soc. Perkin Trans. 1, 1, 3215-3237.
    • (1999) J. Chem. Soc. Perkin Trans , vol.1 , pp. 3215-3237
    • Davis, B.1
  • 5
    • 0020443962 scopus 로고
    • Dual role of hexose-1-phosphate uridylyltransferase in galactosamine metabolism
    • Weckbecker, G. and Keppler, D.O. (1982) Dual role of hexose-1-phosphate uridylyltransferase in galactosamine metabolism. Eur. J. Biochem., 128, 163-168.
    • (1982) Eur. J. Biochem. , vol.128 , pp. 163-168
    • Weckbecker, G.1    Keppler, D.O.2
  • 6
    • 0035805630 scopus 로고    scopus 로고
    • Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site
    • Thoden, J.B., Wohlers, T.M., Fridovich-Keil, J.L. and Holden, H.M. (2001) Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site. J. Biol. Chem., 276, 15131-15136.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15131-15136
    • Thoden, J.B.1    Wohlers, T.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 8
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:Polypeptide N-acetylgalactosaminyltransferases
    • Ten Hagen, K.G., Fritz, T. and Tabak, L. (2003) All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology, 13, 1R-16R.
    • (2003) Glycobiology , vol.13 , pp. 1R-16R
    • Ten Hagen, K.G.1    Fritz, T.2    Tabak, L.3
  • 9
    • 30744451472 scopus 로고    scopus 로고
    • Glycosaminoglycans and their proteoglycans: Host-associated molecular patterns for initiation and modulation of inflammation
    • Taylor, K.R. and Gallo, R.L. (2006) Glycosaminoglycans and their proteoglycans: host-associated molecular patterns for initiation and modulation of inflammation. Faseb J., 20, 9-22.
    • (2006) Faseb J. , vol.20 , pp. 9-22
    • Taylor, K.R.1    Gallo, R.L.2
  • 10
    • 77449135166 scopus 로고    scopus 로고
    • Galactose toxicity in animals
    • Lai, K., Elsas, L.J. and Wierenga, K.J. (2009) Galactose toxicity in animals. IUBMB Life, 61, 1063-1074.
    • (2009) IUBMB Life , vol.61 , pp. 1063-1074
    • Lai, K.1    Elsas, L.J.2    Wierenga, K.J.3
  • 11
    • 84055217127 scopus 로고    scopus 로고
    • Structural and molecular biology of type I galactosemia: Disease-associated mutations
    • McCorvie, T.J. and Timson, D.J. (2011) Structural and molecular biology of type I galactosemia: disease-associated mutations. IUBMB Life, 63, 949-954.
    • (2011) IUBMB Life , vol.63 , pp. 949-954
    • McCorvie, T.J.1    Timson, D.J.2
  • 14
    • 0001614395 scopus 로고
    • Galactose-1-phosphate in galactosemia
    • Donnell, G., Bergren, W., Perry, G. and Koch, R. (1963) Galactose-1-phosphate in galactosemia. Pediatrics, 31, 802-810.
    • (1963) Pediatrics , vol.31 , pp. 802-810
    • Donnell, G.1    Bergren, W.2    Perry, G.3    Koch, R.4
  • 15
    • 0037718404 scopus 로고    scopus 로고
    • GALT deficiency causes UDP-hexose deficit in human galactosemic cells
    • Lai, K., Langley, S.D., Khwaja, F.W., Schmitt, E.W. and Elsas, L.J. (2003) GALT deficiency causes UDP-hexose deficit in human galactosemic cells. Glycobiology, 13, 285-294.
    • (2003) Glycobiology , vol.13 , pp. 285-294
    • Lai, K.1    Langley, S.D.2    Khwaja, F.W.3    Schmitt, E.W.4    Elsas, L.J.5
  • 17
    • 84856637730 scopus 로고    scopus 로고
    • Differential glycomics of epithelial membrane glycoproteins from urinary exovesicles reveals shifts toward complex-type N-glycosylation in classical galactosemia
    • Staubach, S., Schadewaldt, P., Wendel, U., Nohroudi, K. and Hanisch, F.G. (2012) Differential glycomics of epithelial membrane glycoproteins from urinary exovesicles reveals shifts toward complex-type N-glycosylation in classical galactosemia. J. Proteome Res., 11, 906-916.
    • (2012) J. Proteome Res. , vol.11 , pp. 906-916
    • Staubach, S.1    Schadewaldt, P.2    Wendel, U.3    Nohroudi, K.4    Hanisch, F.G.5
  • 20
    • 34948901347 scopus 로고    scopus 로고
    • Mutation database for the galactose-1-phosphate uridyltransferase (GALT) gene
    • Calderon, F.R.O., Phansalkar, A.R., Crockett, D.K., Miller, M. and Mao, R. (2007) Mutation database for the galactose-1-phosphate uridyltransferase (GALT) gene. Hum. Mutat., 28, 939-943.
    • (2007) Hum. Mutat. , vol.28 , pp. 939-943
    • Calderon, F.R.O.1    Phansalkar, A.R.2    Crockett, D.K.3    Miller, M.4    Mao, R.5
  • 21
    • 80052098383 scopus 로고    scopus 로고
    • The structural and molecular biology of type i galactosemia: Enzymology of galactose 1-phosphate uridylyltransferase
    • McCorvie, T.J. and Timson, D.J. (2011) The structural and molecular biology of type i galactosemia: enzymology of galactose 1-phosphate uridylyltransferase. IUBMB Life, 63, 694-700.
    • (2011) IUBMB Life , vol.63 , pp. 694-700
    • McCorvie, T.J.1    Timson, D.J.2
  • 22
    • 0037162392 scopus 로고    scopus 로고
    • Hint, Fhit, and GalT: Function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases
    • Brenner, C. (2002) Hint, Fhit, and GalT: Function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Biochemistry, 41, 9003-9014.
    • (2002) Biochemistry , vol.41 , pp. 9003-9014
    • Brenner, C.1
  • 23
    • 0029113143 scopus 로고
    • Threedimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution
    • Wedekind, J.E., Frey, P.A. and Rayment, I. (1995) Threedimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution. Biochemistry, 34, 11049-11061.
    • (1995) Biochemistry , vol.34 , pp. 11049-11061
    • Wedekind, J.E.1    Frey, P.A.2    Rayment, I.3
  • 24
    • 0029810819 scopus 로고    scopus 로고
    • The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer
    • Wedekind, J.E., Frey, P.A. and Rayment, I. (1996) The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer. Biochemistry, 35, 11560-11569.
    • (1996) Biochemistry , vol.35 , pp. 11560-11569
    • Wedekind, J.E.1    Frey, P.A.2    Rayment, I.3
  • 25
    • 0031019959 scopus 로고    scopus 로고
    • Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: Detailed description of the nucleotide sugar binding site
    • Thoden, J.B., Ruzicka, F.J., Frey, P.A., Rayment, I. and Holden, H.M. (1997) Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site. Biochemistry, 36, 1212-1222.
    • (1997) Biochemistry , vol.36 , pp. 1212-1222
    • Thoden, J.B.1    Ruzicka, F.J.2    Frey, P.A.3    Rayment, I.4    Holden, H.M.5
  • 26
    • 0032829746 scopus 로고    scopus 로고
    • Significance of metal ions in galactose-1-phosphate uridylyltransferase: An essential structural zinc and a nonessential structural iron
    • Geeganage, S. and Frey, P.A. (1999) Significance of metal ions in galactose-1-phosphate uridylyltransferase: an essential structural zinc and a nonessential structural iron. Biochemistry, 38, 13398-13406.
    • (1999) Biochemistry , vol.38 , pp. 13398-13406
    • Geeganage, S.1    Frey, P.A.2
  • 27
    • 0030869976 scopus 로고    scopus 로고
    • Biochemical characterization of the S135L allele of galactose-1-phosphate uridyilyltransferase associated with galactosaemia
    • Wells, L. and FridovichKeil, J.L. (1997) Biochemical characterization of the S135L allele of galactose-1-phosphate uridyilyltransferase associated with galactosaemia. J. Inherit. Metab. Dis., 20, 633-642.
    • (1997) J. Inherit. Metab. Dis. , vol.20 , pp. 633-642
    • Wells, L.1    FridovichKeil, J.L.2
  • 28
    • 13444291908 scopus 로고    scopus 로고
    • Homology modeling studies on human galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo-and heterodimers
    • Marabotti, A. and Facchiano, A.M. (2005) Homology modeling studies on human galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo-and heterodimers. J. Med. Chem., 48, 773-779.
    • (2005) J. Med. Chem. , vol.48 , pp. 773-779
    • Marabotti, A.1    Facchiano, A.M.2
  • 29
    • 75649089285 scopus 로고    scopus 로고
    • Analysis of galactosemia-linked mutations of GALT enzyme using a computational biology approach
    • Facchiano, A. and Marabotti, A. (2010) Analysis of galactosemia-linked mutations of GALT enzyme using a computational biology approach. Protein Eng. Des. Sel., 23, 103-113.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 103-113
    • Facchiano, A.1    Marabotti, A.2
  • 32
    • 0034730499 scopus 로고    scopus 로고
    • Covalent heterogeneity of the human enzyme galactose-1-phosphate uridylyltransferase
    • Henderson, J.M., Wells, L. and Fridovich-Keil, J.L. (2000) Covalent heterogeneity of the human enzyme galactose-1-phosphate uridylyltransferase. J. Biol. Chem., 275, 30088-30091.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30088-30091
    • Henderson, J.M.1    Wells, L.2    Fridovich-Keil, J.L.3
  • 33
    • 40849114576 scopus 로고    scopus 로고
    • A yeast model reveals biochemical severity associated with each of three variant alleles of galactose-1P uridylyltransferase segregating in a single family
    • Chhay, J.S., Openo, K.K., Eaton, J.S., Gentile, M. and Fridovich-Keil, J.L. (2008) A yeast model reveals biochemical severity associated with each of three variant alleles of galactose-1P uridylyltransferase segregating in a single family. J. Inherit. Metab. Dis., 31, 97-107.
    • (2008) J. Inherit. Metab. Dis. , vol.31 , pp. 97-107
    • Chhay, J.S.1    Openo, K.K.2    Eaton, J.S.3    Gentile, M.4    Fridovich-Keil, J.L.5
  • 34
    • 0034788782 scopus 로고    scopus 로고
    • Structure-function analyses of a common mutation in blacks with transferase-deficiency galactosemia
    • Lai, K. and Elsas, L.J. (2001) Structure-function analyses of a common mutation in blacks with transferase-deficiency galactosemia. Mol. Genet. Metab., 74, 264-272.
    • (2001) Mol. Genet. Metab. , vol.74 , pp. 264-272
    • Lai, K.1    Elsas, L.J.2
  • 35
    • 0033525873 scopus 로고    scopus 로고
    • The biochemical role of glutamine 188 in human galactose-1-phosphate uridyltransferase
    • Lai, K., Willis, A.C. and Elsas, L.J. (1999) The biochemical role of glutamine 188 in human galactose-1-phosphate uridyltransferase. J. Biol. Chem., 274, 6559-6566.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6559-6566
    • Lai, K.1    Willis, A.C.2    Elsas, L.J.3
  • 37
    • 67649666838 scopus 로고    scopus 로고
    • GALT protein database, a bioinformatics resource for the management and analysis of structural features of a galactosemiarelated protein and its mutants
    • Acierno, A., Facchiano, A. and Marabotti, A. (2009) GALT protein database, a bioinformatics resource for the management and analysis of structural features of a galactosemiarelated protein and its mutants. Genomics Proteomics Bioinformatics, 7, 71-76.
    • (2009) Genomics Proteomics Bioinformatics , vol.7 , pp. 71-76
    • Acierno, A.1    Facchiano, A.2    Marabotti, A.3
  • 38
    • 84998738352 scopus 로고    scopus 로고
    • Cofactors and metabolites as protein folding helpers in metabolic diseases
    • Rodrigues, J.V., Henriques, B.J., Lucas, T.G. and Gomes, C.M. (2013) Cofactors and metabolites as protein folding helpers in metabolic diseases. Curr. Top. Med. Chem., 999, 29-35.
    • (2013) Curr. Top. Med. Chem. , vol.999 , pp. 29-35
    • Rodrigues, J.V.1    Henriques, B.J.2    Lucas, T.G.3    Gomes, C.M.4
  • 39
    • 84861886186 scopus 로고    scopus 로고
    • Correlation assessment among clinical phenotypes, expression analysis and molecular modeling of 14 novel variations in the human galactose-1-phosphate uridylyltransferase gene
    • Tang, M., Facchiano, A., Rachamadugu, R., Calderon, F., Mao, R., Milanesi, L., Marabotti, A. and Lai, K. (2012) Correlation assessment among clinical phenotypes, expression analysis and molecular modeling of 14 novel variations in the human galactose-1-phosphate uridylyltransferase gene. Hum. Mutat., 33, 1107-1115.
    • (2012) Hum. Mutat. , vol.33 , pp. 1107-1115
    • Tang, M.1    Facchiano, A.2    Rachamadugu, R.3    Calderon, F.4    Mao, R.5    Milanesi, L.6    Marabotti, A.7    Lai, K.8
  • 41
    • 10544248591 scopus 로고    scopus 로고
    • The Q188R mutation in human galactose-1-phosphate uridylyltransferase acts as a partial dominant negative
    • Elsevier, J.P. and Fridovich-Keil, J.L. (1996) The Q188R mutation in human galactose-1-phosphate uridylyltransferase acts as a partial dominant negative. J. Biol. Chem., 271, 32002-32007.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32002-32007
    • Elsevier, J.P.1    Fridovich-Keil, J.L.2
  • 42
    • 84883174258 scopus 로고    scopus 로고
    • The role of protein denaturation energetics and molecular chaperones in the aggregation and mistargeting of mutants causing primary hyperoxaluria type I
    • Mesa-Torres, N., Fabelo-Rosa, I., Riverol, D., Yunta, C., Albert, A., Salido, E. and Pey, A.L. (2013) The role of protein denaturation energetics and molecular chaperones in the aggregation and mistargeting of mutants causing primary hyperoxaluria type I. PLoS One, 8, e71963.
    • (2013) PLoS One , vol.8 , pp. e71963
    • Mesa-Torres, N.1    Fabelo-Rosa, I.2    Riverol, D.3    Yunta, C.4    Albert, A.5    Salido, E.6    Pey, A.L.7
  • 43
    • 84911435512 scopus 로고    scopus 로고
    • Compromised catalysis and potential folding defects in in vitro studies of missense mutants associated with hereditary phosphoglucomutase 1 deficiency
    • Lee, Y., Stiers, K.M., Kain, B.N. and Beamer, L.J. (2014) Compromised catalysis and potential folding defects in in vitro studies of missense mutants associated with hereditary phosphoglucomutase 1 deficiency. J. Biol. Chem., 289, 32010-32019.
    • (2014) J. Biol. Chem. , vol.289 , pp. 32010-32019
    • Lee, Y.1    Stiers, K.M.2    Kain, B.N.3    Beamer, L.J.4
  • 44
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • Valentine, J.S., Doucette, P.A. and Zittin Potter, S. (2005) Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu. Rev. Biochem., 74, 563-593.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 45
    • 77954681706 scopus 로고    scopus 로고
    • The missing zinc: P53 misfolding and cancer
    • Loh, S.N. (2010) The missing zinc: p53 misfolding and cancer. Metallomics, 2, 442-449.
    • (2010) Metallomics , vol.2 , pp. 442-449
    • Loh, S.N.1
  • 46
    • 59449095419 scopus 로고    scopus 로고
    • Molecular aspects of human cellular zinc homeostasis: Redox control of zinc potentials and zinc signals
    • Maret, W. (2009) Molecular aspects of human cellular zinc homeostasis: redox control of zinc potentials and zinc signals. BioMetals, 22, 149-157.
    • (2009) BioMetals , vol.22 , pp. 149-157
    • Maret, W.1
  • 47
    • 84897366805 scopus 로고    scopus 로고
    • Zinc homeostasis and neurodegenerative disorders
    • Szewczyk, B. (2013) Zinc homeostasis and neurodegenerative disorders. Front. Aging Neurosci., 5, 33.
    • (2013) Front. Aging Neurosci. , vol.5 , pp. 33
    • Szewczyk, B.1
  • 51
    • 79952548103 scopus 로고    scopus 로고
    • Phenylketonuria as a model for protein misfolding diseases and for the development of next generation orphan drugs for patients with inborn errors of metabolism
    • Muntau, A. and Gersting, S. (2010) Phenylketonuria as a model for protein misfolding diseases and for the development of next generation orphan drugs for patients with inborn errors of metabolism. J. Inherit. Metab. Dis., 33, 649-658.
    • (2010) J. Inherit. Metab. Dis. , vol.33 , pp. 649-658
    • Muntau, A.1    Gersting, S.2
  • 52
    • 79957628617 scopus 로고    scopus 로고
    • Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders
    • Valenzano, K.J., Khanna, R., Powe, A.C., Boyd, R., Lee, G., Flanagan, J.J. and Benjamin, E.R. (2011) Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders. Assay Drug Dev. Technol., 9, 213-235.
    • (2011) Assay Drug Dev. Technol. , vol.9 , pp. 213-235
    • Valenzano, K.J.1    Khanna, R.2    Powe, A.C.3    Boyd, R.4    Lee, G.5    Flanagan, J.J.6    Benjamin, E.R.7
  • 53
    • 84983550060 scopus 로고    scopus 로고
    • Arginine Functionally Improves Clinically Relevant Human Galactose-1-Phosphate Uridylyltransferase (GALT) Variants Expressed in a Prokaryotic Model
    • Coelho, A., Trabuco, M., Silva, M., De Almeida, I.T., Leandro, P., Rivera, I. and Vicente, J.B. (2015) Arginine Functionally Improves Clinically Relevant Human Galactose-1-Phosphate Uridylyltransferase (GALT) Variants Expressed in a Prokaryotic Model. JIMD Rep., 23, 1-6.
    • (2015) JIMD Rep. , vol.23 , pp. 1-6
    • Coelho, A.1    Trabuco, M.2    Silva, M.3    De Almeida, I.T.4    Leandro, P.5    Rivera, I.6    Vicente, J.B.7
  • 54
    • 14844361966 scopus 로고    scopus 로고
    • Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation
    • Ray, S., Nowak, R., Brown, R.J. and Lansbury, P.J. (2005) Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. Proc. Natl. Acad. Sci. USA., 102, 3639-3644.
    • (2005) Proc. Natl. Acad. Sci. USA. , vol.102 , pp. 3639-3644
    • Ray, S.1    Nowak, R.2    Brown, R.J.3    Lansbury, P.J.4
  • 56
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (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
  • 61
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen, F.H., Berglund, H. and Vedadi, M. (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc., 2, 2212-2221.
    • (2007) Nat. Protoc. , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.