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Volumn 17, Issue 9, 1998, Pages 2463-2471

Crystal structure of human uroporphyrinogen decarboxylase

Author keywords

Coproporphyrinogen; Heme; PCT; Porphyria cutanea tarda; Porphyrin

Indexed keywords

ARGININE; ASPARTIC ACID; COPROPORPHYRINOGEN; DIMER; HISTIDINE; RECOMBINANT ENZYME; SERINE; TYROSINE; UROPORPHYRINOGEN; UROPORPHYRINOGEN DECARBOXYLASE;

EID: 0032079342     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.9.2463     Document Type: Article
Times cited : (90)

References (42)
  • 1
    • 0011985458 scopus 로고
    • Stereochemistry of porphyrinogen carboxy-lyase reaction in haem biosynthesis
    • Barnard,G.F. and Akhtar,M. (1975) Stereochemistry of porphyrinogen carboxy-lyase reaction in haem biosynthesis. J. Chem. Soc. Chem. Commun., 10, 494-496.
    • (1975) J. Chem. Soc. Chem. Commun. , vol.10 , pp. 494-496
    • Barnard, G.F.1    Akhtar, M.2
  • 2
    • 0018557757 scopus 로고
    • Stereochemical and mechanistic studies on the decarboxylation of uroporphyrinogen III in haem biosynthesis
    • Barnard,G.F. and Akhtar,M. (1979) Stereochemical and mechanistic studies on the decarboxylation of uroporphyrinogen III in haem biosynthesis. J. Chem. Soc. Perkin Trans. 1, 13, 2354-2360.
    • (1979) J. Chem. Soc. Perkin Trans. 1 , vol.13 , pp. 2354-2360
    • Barnard, G.F.1    Akhtar, M.2
  • 3
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Briinger,A.T. (1992) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Briinger, A.T.1
  • 5
    • 0027052739 scopus 로고
    • Identification of amino acid changes affecting yeast uroporphyrinogen decarboxylase activity by sequence analysis of hem12 mutant alleles
    • Chelstowska,A., Zoladek,T., Garey,J., Kushner,J., Rytka,J. and Labbe-Bois,R. (1992) Identification of amino acid changes affecting yeast uroporphyrinogen decarboxylase activity by sequence analysis of hem12 mutant alleles. Biochem. J., 288, 753-757.
    • (1992) Biochem. J. , vol.288 , pp. 753-757
    • Chelstowska, A.1    Zoladek, T.2    Garey, J.3    Kushner, J.4    Rytka, J.5    Labbe-Bois, R.6
  • 6
    • 0018900912 scopus 로고
    • Some kinetic properties of human red cell uroporphyrinogen decarboxylase
    • de Verneuil,H., Grandchamp,B. and Nordmann,Y. (1980) Some kinetic properties of human red cell uroporphyrinogen decarboxylase. Biochim. Biophys. Acta, 611, 174-186.
    • (1980) Biochim. Biophys. Acta , vol.611 , pp. 174-186
    • De Verneuil, H.1    Grandchamp, B.2    Nordmann, Y.3
  • 7
    • 0021321665 scopus 로고
    • Assignment of the gene for uroporphyrinogen decarboxylase to human chromosome 1 by somatic cell hybridization and specific enzyme immunoassay
    • de Verneuil,H., Grandchamp,B., Foubert,C., Weil,D., N'Guyen,V.C., Gross,M.S., Sassa,S. and Nordmann,Y. (1984) Assignment of the gene for uroporphyrinogen decarboxylase to human chromosome 1 by somatic cell hybridization and specific enzyme immunoassay. Hum. Genet., 66, 202-205.
    • (1984) Hum. Genet. , vol.66 , pp. 202-205
    • De Verneuil, H.1    Grandchamp, B.2    Foubert, C.3    Weil, D.4    N'Guyen, V.C.5    Gross, M.S.6    Sassa, S.7    Nordmann, Y.8
  • 9
    • 0018070910 scopus 로고
    • Decreased activity of hepatic uroporphyrinogen decarboxylase in sporadic porphyria cutanea tarda
    • Elder,G.H., Lee,G.B. and Tovey,J.A. (1978) Decreased activity of hepatic uroporphyrinogen decarboxylase in sporadic porphyria cutanea tarda. N. Engl. J. Med., 299, 274-278.
    • (1978) N. Engl. J. Med. , vol.299 , pp. 274-278
    • Elder, G.H.1    Lee, G.B.2    Tovey, J.A.3
  • 11
    • 0024549625 scopus 로고
    • A point mutation in the coding region of uroporphyrinogen decarboxylase associated with familial porphyria cutanea tarda
    • Garey,J.R., Hansen,J.L., Harrison,L.M., Kennedy,J.B. and Kushner,J.P. (1989) A point mutation in the coding region of uroporphyrinogen decarboxylase associated with familial porphyria cutanea tarda. Blood, 73, 892-895.
    • (1989) Blood , vol.73 , pp. 892-895
    • Garey, J.R.1    Hansen, J.L.2    Harrison, L.M.3    Kennedy, J.B.4    Kushner, J.P.5
  • 12
  • 13
    • 0030765455 scopus 로고    scopus 로고
    • Dali/FSSP classification of three-dimensional protein folds
    • Holm,L. and Sander,C. (1997) Dali/FSSP classification of three-dimensional protein folds. Nucleic Acids Res., 25, 231-234.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 231-234
    • Holm, L.1    Sander, C.2
  • 14
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson,E.G. and Thornton,J.M. (1996) PROMOTIF - a program to identify and analyze structural motifs in proteins. Protein Sci., 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 16
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution
    • Johnston,S.C., Larsen,C.N., Cook,W.J., Wilkinson,K.D. and Hill,C.P. (1997) Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution. EMBO J., 16, 3787-3796.
    • (1997) EMBO J. , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones,T.A., Zou,J.-Y., Cowan,S.W. and Kjeldgaard,M. (1991) Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0020569127 scopus 로고
    • Uroporphyrinogen decarboxylase. Purification, properties, and inhibition by poly chlorinated biphenyl isomers
    • Kawanishi,S., Seki,Y. and Sano,S. (1983) Uroporphyrinogen decarboxylase. Purification, properties, and inhibition by poly chlorinated biphenyl isomers. J. Biol. Chem., 258, 4285-4292.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4285-4292
    • Kawanishi, S.1    Seki, Y.2    Sano, S.3
  • 20
    • 0023085460 scopus 로고
    • Biosythesis of porphyrins in Rhodoseudomonas palustris. VI. the effect of metals, thiols, and other reagents on the activity of uroporphyrinogen decarboxylase
    • Koopman,G.E. and Battle,A.d.C. (1987) Biosythesis of porphyrins in Rhodoseudomonas palustris. VI. The effect of metals, thiols, and other reagents on the activity of uroporphyrinogen decarboxylase. Int. J. Biochem., 19, 373-377.
    • (1987) Int. J. Biochem. , vol.19 , pp. 373-377
    • Koopman, G.E.1    Battle, A.D.C.2
  • 21
    • 0017168895 scopus 로고
    • An inherited enzymatic defect in porphyria cutanea tarda: Decreased uroporphyrinogen decarboxylase activity
    • Kushner,J.P, Barbuto,A.J. and Lee,G.R. (1976) An inherited enzymatic defect in porphyria cutanea tarda: decreased uroporphyrinogen decarboxylase activity. J. Clin. Invest., 58, 1089-1097.
    • (1976) J. Clin. Invest. , vol.58 , pp. 1089-1097
    • Kushner, J.P.1    Barbuto, A.J.2    Lee, G.R.3
  • 22
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the Stereochemical quality of protein structures
    • Laskowski,R.A., MacArthur,M.W., Moss,D.S. and Thornton,J.M. (1993) PROCHECK: a program to check the Stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (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
  • 23
    • 0024529940 scopus 로고
    • Structural principles of α/β barrel proteins: The packing of the interior of the sheet
    • Lesk,A.M., Branden,C.-I, and Chothia,C. (1989) Structural principles of α/β barrel proteins: the packing of the interior of the sheet. Protein Struct. Funct. Genet., 5, 139-148.
    • (1989) Protein Struct. Funct. Genet. , vol.5 , pp. 139-148
    • Lesk, A.M.1    Branden, C.-I.2    Chothia, C.3
  • 24
    • 0022982155 scopus 로고
    • Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4 Å resolution
    • Lim,L.W., Shamala,N., Mathews,F.S., Steenkamp,D.J., Hamlin,R. and Xuong,N.H. (1986) Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4 Å resolution. J. Biol. Chem., 261, 15140-15146.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15140-15146
    • Lim, L.W.1    Shamala, N.2    Mathews, F.S.3    Steenkamp, D.J.4    Hamlin, R.5    Xuong, N.H.6
  • 25
    • 0027473776 scopus 로고
    • Order of uroporphyrinogen III decarboxylation on incubation of porphobilinogen and uroporphyrinogen ITT with erythrocyte uroporphyrinogen decarboxylase
    • Luo,J. and Lim,C.K. (1993) Order of uroporphyrinogen III decarboxylation on incubation of porphobilinogen and uroporphyrinogen ITT with erythrocyte uroporphyrinogen decarboxylase. Biochem. J., 289, 529-532.
    • (1993) Biochem. J. , vol.289 , pp. 529-532
    • Luo, J.1    Lim, C.K.2
  • 26
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Marthews,B.W. (1968) Solvent content of protein crystals. J. Mol. Biol., 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Marthews, B.W.1
  • 27
    • 0029858578 scopus 로고    scopus 로고
    • Five new mutations in the uroporphyrinogen decarboxylase gene identified in families with cutaneous porphyria
    • McManus,J.F., Begley,C.G., Sassa,S. and Ratnaike,S. (1996) Five new mutations in the uroporphyrinogen decarboxylase gene identified in families with cutaneous porphyria. Blood, 88, 3589-3600.
    • (1996) Blood , vol.88 , pp. 3589-3600
    • McManus, J.F.1    Begley, C.G.2    Sassa, S.3    Ratnaike, S.4
  • 28
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/XView
    • McRee,D.E. (1992) A visual protein crystallographic software system for X11/XView. J. Mol. Graphics, 10, 44-46.
    • (1992) J. Mol. Graphics , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 29
    • 0028211449 scopus 로고
    • Molecular defects of uroporphyrinogen decarboxylase in a patient with mild hepatoerythropoietic porphyria
    • Meguro,K. et al. (1994) Molecular defects of uroporphyrinogen decarboxylase in a patient with mild hepatoerythropoietic porphyria. J. Invest. Dermatol., 102, 681-685.
    • (1994) J. Invest. Dermatol. , vol.102 , pp. 681-685
    • Meguro, K.1
  • 31
    • 0028330220 scopus 로고
    • Principles determining the structure of β-sheet barrels in proteins
    • Murzin,A.G., Lesk,A.M. and Chothia,C. (1994) Principles determining the structure of β-sheet barrels in proteins. J. Mol. Biol., 236, 1382-1400.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1382-1400
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 32
    • 0027525607 scopus 로고
    • Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12
    • Nishimura,K., Nakayashiki,T. and Inokuchi,H. (1993) Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12. Gene, 133, 109-113.
    • (1993) Gene , vol.133 , pp. 109-113
    • Nishimura, K.1    Nakayashiki, T.2    Inokuchi, H.3
  • 33
    • 0002452464 scopus 로고
    • Sawyer,L. Isaacs,N. and Bailey,S. (eds), SERC Daresbury Laboratory, Warrington UK
    • Otwinowski,Z. (1993) Oscillation data reduction program. In Sawyer,L. Isaacs,N. and Bailey,S. (eds), SERC Daresbury Laboratory, Warrington UK, pp. 56-62.
    • (1993) Oscillation Data Reduction Program. , pp. 56-62
    • Otwinowski, Z.1
  • 34
    • 0031008511 scopus 로고    scopus 로고
    • Characterization and crystallization of human uroporphyrinogen decarboxylase
    • Phillips,J.D., Whiiby,F.G., Kushner,J.P and Hill,C.P. (1997) Characterization and crystallization of human uroporphyrinogen decarboxylase. Protein Sci., 6, 1343-1346.
    • (1997) Protein Sci. , vol.6 , pp. 1343-1346
    • Phillips, J.D.1    Whiiby, F.G.2    Kushner, J.P.3    Hill, C.P.4
  • 35
    • 0031045818 scopus 로고    scopus 로고
    • Treatment of multiwavelength anomalous diffraction as a special case of multiple isomorphous replacement
    • Ramakrishnan,V. and Biou,V. (1997) Treatment of multiwavelength anomalous diffraction as a special case of multiple isomorphous replacement. Methods Enzymol., 276, 538-557.
    • (1997) Methods Enzymol. , vol.276 , pp. 538-557
    • Ramakrishnan, V.1    Biou, V.2
  • 38
    • 0022559022 scopus 로고
    • Uroporphyrinogen decarboxylase purification from chicken erythrocytes
    • Seki,Y., Kawanishi,S. and Sano,S. (1986) Uroporphyrinogen decarboxylase purification from chicken erythrocytes. Methods Enzymol., 123, 415-421.
    • (1986) Methods Enzymol. , vol.123 , pp. 415-421
    • Seki, Y.1    Kawanishi, S.2    Sano, S.3
  • 39
    • 0028052114 scopus 로고
    • 8 proteins using hydrogen-bonding pattern
    • 8 proteins using hydrogen-bonding pattern. J. Mol. Biol., 244, 168-182.
    • (1994) J. Mol. Biol. , vol.244 , pp. 168-182
    • Sergeev, Y.1    Lee, B.2
  • 40
    • 0020407640 scopus 로고
    • Uroporphyrinogen decarboxylase: A method for measuring enzymatic activity
    • Straka,J.G., Kushner,J.P. and Pryor,M.A. (1982) Uroporphyrinogen decarboxylase: a method for measuring enzymatic activity. Enzyme, 28, 170-185.
    • (1982) Enzyme , vol.28 , pp. 170-185
    • Straka, J.G.1    Kushner, J.P.2    Pryor, M.A.3
  • 41
    • 0002698015 scopus 로고
    • Heme biosynthesis, the porphyrias, and the liver
    • Arias,I.M., Boyer,J.L., Fausto,N., Jakoby,W.B., Schachter,D.A. and ShafritzD.A. (eds), Raven Press, Ltd, New York
    • Wyckoff,E.E. and Kushner,J.P. (1994) Heme biosynthesis, the porphyrias, and the liver. In Arias,I.M., Boyer,J.L., Fausto,N., Jakoby,W.B., Schachter,D.A. and ShafritzD.A. (eds), The Liver: Biology and Pathobiology. Raven Press, Ltd, New York, pp. 505-527.
    • (1994) The Liver: Biology and Pathobiology , pp. 505-527
    • Wyckoff, E.E.1    Kushner, J.P.2


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