메뉴 건너뛰기




Volumn 244, Issue 2, 1997, Pages 407-413

Reversible folding of UDP-galactose 4-epimerase from Escherichia coli

Author keywords

Denaturation; Escherichia coli; Protein folding; UDP galactose 4 epimerase; Urea

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 0031053442     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00407.x     Document Type: Article
Times cited : (15)

References (25)
  • 2
    • 0001757004 scopus 로고
    • The interconversion of monosaccharides
    • Gabriel, O. & Lanten, L. V. (1978) The interconversion of monosaccharides, Int. Rev. Biochem. 16, 1-36.
    • (1978) Int. Rev. Biochem. , vol.16 , pp. 1-36
    • Gabriel, O.1    Lanten, L.V.2
  • 3
    • 0001555950 scopus 로고
    • Complex pyridine nucleotide dependent transformations
    • (Dolphin, D., Poulson, R. & Avarmovie, O., eds) Wiley, New York
    • Frey, P. A. (1987) Complex pyridine nucleotide dependent transformations, in Pyridine nucleotide coenzymes: chemical, biochemical and medical aspects (Dolphin, D., Poulson, R. & Avarmovie, O., eds) vol. 2B, pp. 462-447, Wiley, New York.
    • (1987) Pyridine Nucleotide Coenzymes: Chemical, Biochemical and Medical Aspects , vol.2 B , pp. 462-1447
    • Frey, P.A.1
  • 4
    • 0023046226 scopus 로고
    • Nucleotide sequence of the gal E gene and the gal T gene of E. coli
    • Lemaire, H. G. & Miller-Hill, B. (1986) Nucleotide sequence of the gal E gene and the gal T gene of E. coli, Nucleic Acids Res. 14, 7705-7711.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 7705-7711
    • Lemaire, H.G.1    Miller-Hill, B.2
  • 5
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 Å resolution
    • Bauer, A. J., Rayment, I., Frey, P. A. & Holden, H. M. (1992) The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 Å resolution, Proteins Struct. Funct. Genet. 12, 372-381.
    • (1992) Proteins Struct. Funct. Genet. , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 6
    • 0017804038 scopus 로고
    • Escherichia coli uridine diphosphate galactose 4-epimerase: Circular dichroism of the protein and protein-bound dihydronicotinamide adenine dinucleotide
    • Wong, S. S., Cassim, J. Y. & Frey, P. A. (1978) Escherichia coli uridine diphosphate galactose 4-epimerase: circular dichroism of the protein and protein-bound dihydronicotinamide adenine dinucleotide, Biochemistry 17, 516-520.
    • (1978) Biochemistry , vol.17 , pp. 516-520
    • Wong, S.S.1    Cassim, J.Y.2    Frey, P.A.3
  • 7
    • 0027740162 scopus 로고
    • Identification of lysine 153 as a functionally important residue in UDP-galactose 4-epimerase from E. coli
    • Swanson, B. A. & Frey, P. A. (1993) Identification of lysine 153 as a functionally important residue in UDP-galactose 4-epimerase from E. coli, Biochemistry 32, 13231-13236.
    • (1993) Biochemistry , vol.32 , pp. 13231-13236
    • Swanson, B.A.1    Frey, P.A.2
  • 8
    • 0027960974 scopus 로고
    • Characterization and activation of naturally occuring abortive complexes of UDP-Galactose 4-epimerase from E. coli
    • Vanhooke, J. L. V. & Frey, P. A. (1994) Characterization and activation of naturally occuring abortive complexes of UDP-Galactose 4-epimerase from E. coli, J. Biol. Chem. 269, 31496-31504.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31496-31504
    • Vanhooke, J.L.V.1    Frey, P.A.2
  • 9
    • 0027371576 scopus 로고
    • Reversible folding of UDP-galactose 4-epimerase from yeast Kluyveromyces fragilis
    • Bhattacharyya, D. (1993) Reversible folding of UDP-galactose 4-epimerase from yeast Kluyveromyces fragilis, Biochemistry 32, 9726-9734.
    • (1993) Biochemistry , vol.32 , pp. 9726-9734
    • Bhattacharyya, D.1
  • 10
    • 0000290994 scopus 로고
    • The enzymes of the galactose operon in Escherichia coli I. Purification and characterization of uridine diphosphogalactose 4-epimerase
    • Wilson, D. B. & Hogness, D. S. (1964) The enzymes of the galactose operon in Escherichia coli I. Purification and characterization of uridine diphosphogalactose 4-epimerase, J. Biol. Chem. 239, 2469-2481.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2469-2481
    • Wilson, D.B.1    Hogness, D.S.2
  • 11
    • 0014289732 scopus 로고
    • Purification and properties of uridine diphospho galactose 4-epimerase from yeast
    • Darrow, R. A. & Rodstrom, R. (1968) Purification and properties of uridine diphospho galactose 4-epimerase from yeast, Biochemistry 7, 1645-1654.
    • (1968) Biochemistry , vol.7 , pp. 1645-1654
    • Darrow, R.A.1    Rodstrom, R.2
  • 12
    • 0021759423 scopus 로고
    • Use of high speed size exclusion chromatography for the study of protein folding and stability
    • Corbett, R. J. J. & Roche, R. S. (1984) Use of high speed size exclusion chromatography for the study of protein folding and stability, Biochemistry 23, 1888-1894.
    • (1984) Biochemistry , vol.23 , pp. 1888-1894
    • Corbett, R.J.J.1    Roche, R.S.2
  • 13
    • 8044250107 scopus 로고
    • Peptides and proteins, 2nd edn
    • CRC Press
    • Handbook of Biochemistry (1970) Peptides and proteins, 2nd edn, CRC Press, C71-C92.
    • (1970) Handbook of Biochemistry
  • 14
    • 0027733616 scopus 로고
    • Use of fast protein size exclusion liquid chromatography to study the unfolding of proteins which denature through molten globule
    • Uversky, V. N. (1993) Use of fast protein size exclusion liquid chromatography to study the unfolding of proteins which denature through molten globule, Biochemistry 32, 13288-13298.
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 15
    • 0000297444 scopus 로고
    • Vitamins coenzymes and their metabolites
    • Academic Press, New York
    • Udenfriend, S. (1962) Vitamins coenzymes and their metabolites, in Fluoresence assay in biology and medicine, vol. 1, p. 249, Academic Press, New York.
    • (1962) Fluoresence Assay in Biology and Medicine , vol.1 , pp. 249
    • Udenfriend, S.1
  • 17
    • 0020787788 scopus 로고
    • Purification of reduced NAD by Ionexchange and high performance liquid chromatography
    • Newton, J. C., Faynor, M. S. & Northrop, B. D. (1983) Purification of reduced NAD by Ionexchange and high performance liquid chromatography, Anal. Biochem. 132, 50-53.
    • (1983) Anal. Biochem. , vol.132 , pp. 50-53
    • Newton, J.C.1    Faynor, M.S.2    Northrop, B.D.3
  • 20
    • 0017889591 scopus 로고
    • Uridine diphosphate galactose 4-epimerase: Nucleotide and 8-anilino 1-naphthalenesulfonate binding properties of the substrate-binding site
    • Wong, S. S. & Frey, P. A. (1978) Uridine diphosphate galactose 4-epimerase: Nucleotide and 8-anilino 1-naphthalenesulfonate binding properties of the substrate-binding site, Biochemistry 17, 3551-3556.
    • (1978) Biochemistry , vol.17 , pp. 3551-3556
    • Wong, S.S.1    Frey, P.A.2
  • 21
    • 0022555910 scopus 로고
    • Kinetic mechanisms of protein folding
    • Utiyama, H. & Baldwin, R. L. (1986) Kinetic mechanisms of protein folding, Methods Enzymol. 131, 51-70.
    • (1986) Methods Enzymol. , vol.131 , pp. 51-70
    • Utiyama, H.1    Baldwin, R.L.2
  • 22
    • 0001848681 scopus 로고
    • Folding of large proteins multidomain and multisubunit proteins
    • (Creighton, T. E., ed.) W. H. Freeman and Company, New York
    • Garel, J. R. (1992) Folding of large proteins multidomain and multisubunit proteins, in Protein folding (Creighton, T. E., ed.) pp. 405-453, W. H. Freeman and Company, New York.
    • (1992) Protein Folding , pp. 405-453
    • Garel, J.R.1
  • 23
    • 0023195509 scopus 로고
    • Mechanism of renaturation of large protein, aspartokinase-homoserine dehydrogenase
    • Vaucheret, H., Signon, L., Le Bras, G. & Garel, J. R. (1987) Mechanism of renaturation of large protein, aspartokinase-homoserine dehydrogenase, Biochemistry 26, 2785-2790.
    • (1987) Biochemistry , vol.26 , pp. 2785-2790
    • Vaucheret, H.1    Signon, L.2    Le Bras, G.3    Garel, J.R.4
  • 24
    • 0029864379 scopus 로고    scopus 로고
    • Collapse and cooperativity in protein folding
    • Miranker, A. D. & Dobson, C. (1996) Collapse and cooperativity in protein folding, Curr. Opin. Struct. Biol. 6, 31-42.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 31-42
    • Miranker, A.D.1    Dobson, C.2
  • 25
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reaction is due to cis-trans isomerism of proline residues
    • Brandts, J. F., Halvarson, H. R. & Brennan, M. (1975) Consideration of the possibility that the slow step in protein denaturation reaction is due to cis-trans isomerism of proline residues, Biochemistry 14, 4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvarson, H.R.2    Brennan, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.