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Volumn 257, Issue 2, 1998, Pages 427-433

UDP-galactose 4-epimerase from Kluyveromyces fragilis: Reconstitution of holoenzyme structure after dissociation with parachloromercuribenzoate

Author keywords

Holoenzyme; Kluyveromyces fragilis; P chloromercuribenzoate; Subunit dissociation; UDP galactose 4 epimerase

Indexed keywords

4 CHLOROMERCURIBENZOIC ACID; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; APOENZYME; DIMER; DITHIOTHREITOL; FUNGAL PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; URIDINE DIPHOSPHATE GALACTOSE; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 0032532538     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2570427.x     Document Type: Article
Times cited : (11)

References (25)
  • 2
    • 0001757004 scopus 로고
    • The interconversion of monosaccharides
    • Gabrial, O. & Lanten, L. V. (1978) The interconversion of monosaccharides, Int. Rev. Biochem. 16, 1-36.
    • (1978) Int. Rev. Biochem. , vol.16 , pp. 1-36
    • Gabrial, 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
    • 0026635537 scopus 로고
    • Distinct functional roles of two active site thiols in UDP-galactose 4-epimerase from Kluyveromyces fragilis
    • Bhattacharjee, H. & Bhaduri, A. (1992) Distinct functional roles of two active site thiols in UDP-galactose 4-epimerase from Kluyveromyces fragilis, J. Biol. Chem. 267, 11714-11720.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11714-11720
    • Bhattacharjee, H.1    Bhaduri, A.2
  • 5
    • 0003024801 scopus 로고
    • Folding-unfolding of oligomeric proteins
    • Academic Press, Orlando, Fl, USA
    • Ghelis, C. & Yon, J. M. (1982) Folding-unfolding of oligomeric proteins, in Protein folding, pp. 470-500, Academic Press, Orlando, Fl, USA.
    • (1982) Protein Folding , pp. 470-500
    • Ghelis, C.1    Yon, J.M.2
  • 6
    • 0022555883 scopus 로고
    • Refolding and association of oligomeric proteins
    • Jaenicke, R. & Rudolph, R. (1986) Refolding and association of oligomeric proteins, Methods Enzymol. 131, 218-250.
    • (1986) Methods Enzymol. , vol.131 , pp. 218-250
    • Jaenicke, R.1    Rudolph, R.2
  • 7
    • 0002101049 scopus 로고
    • Assembly of multi-subunit structures
    • Pain, R. H., ed. Oxford University Press
    • Price, N. C. (1993) Assembly of multi-subunit structures, in Mechanisms of protein folding (Pain, R. H., ed.) pp. 160-193, Oxford University Press.
    • (1993) Mechanisms of Protein Folding , pp. 160-193
    • Price, N.C.1
  • 8
    • 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
  • 9
    • 0014961842 scopus 로고
    • Uridine diphosphate galactose 4-epimerase from Saccharomyces fragilis: Studies on the relationship between quarternary structure and catalytic activity
    • Darrow, R. A. & Rodstrom, R. (1970) Uridine diphosphate galactose 4-epimerase from Saccharomyces fragilis: Studies on the relationship between quarternary structure and catalytic activity, J. Biol. Chem. 145, 2036-2042.
    • (1970) J. Biol. Chem. , vol.145 , pp. 2036-2042
    • Darrow, R.A.1    Rodstrom, R.2
  • 10
    • 0013869228 scopus 로고
    • Subunit association and subunit assembly of uridine diphosphate galactose 4-epimerase from yeast
    • Darrow, R. A. & Rodstrom, R. (1966) Subunit association and subunit assembly of uridine diphosphate galactose 4-epimerase from yeast, Proc. Natl Acad. Sci. USA 55, 205-212.
    • (1966) Proc. Natl Acad. Sci. USA , vol.55 , pp. 205-212
    • Darrow, R.A.1    Rodstrom, R.2
  • 11
    • 0019122769 scopus 로고
    • Presence of two conformationally vicinal sulfydryl groups at the active site of UDP-galactose 4-epimerase from Sacharomyces fragilis
    • Ray, M. & Bhaduri, A. (1980) Presence of two conformationally vicinal sulfydryl groups at the active site of UDP-galactose 4-epimerase from Sacharomyces fragilis, J. Biol. Chem. 255, 10777-10781.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10777-10781
    • Ray, M.1    Bhaduri, A.2
  • 12
    • 0014289732 scopus 로고
    • Purification and properties of uridine diphosphate galactose 4-epimerase from yeast
    • Darrow, R. A. & Rodstrom, R. (1968) Purification and properties of uridine diphosphate galactose 4-epimerase from yeast, Biochemistry 7, 1645-1654.
    • (1968) Biochemistry , vol.7 , pp. 1645-1654
    • Darrow, R.A.1    Rodstrom, R.2
  • 13
    • 0020667655 scopus 로고
    • High-performance liquid chromatography of proteins
    • Regnier, F. E. (1983) High-performance liquid chromatography of proteins, Methods Enzymol. 91, 137-190.
    • (1983) Methods Enzymol. , vol.91 , pp. 137-190
    • Regnier, F.E.1
  • 16
    • 0028230082 scopus 로고
    • Dissociation of enzyme oligomers: A mechanism for allosteric regulation
    • Traut, T. W. (1994) Dissociation of enzyme oligomers: A mechanism for allosteric regulation, Crit. Rev. Biochem. Mol. Biol. 29, 125-163.
    • (1994) Crit. Rev. Biochem. Mol. Biol. , vol.29 , pp. 125-163
    • Traut, T.W.1
  • 17
    • 0020480481 scopus 로고
    • Anilinonaphthalene sulfonate as a probe of membrane composition and function
    • Slavik, J. (1992) Anilinonaphthalene sulfonate as a probe of membrane composition and function, Biochim. Biophys. Acta 694, 1-25.
    • (1992) Biochim. Biophys. Acta , vol.694 , pp. 1-25
    • Slavik, J.1
  • 18
    • 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
  • 19
    • 0020314525 scopus 로고
    • Interaction of 8-anilino 1-naphthalene sulphonic acid with UDP-galactose 4-epimerase from Saccharomyces fragilis
    • Samanta, A. K. & Bhaduri, A. (1982) Interaction of 8-anilino 1-naphthalene sulphonic acid with UDP-galactose 4-epimerase from Saccharomyces fragilis, Ind. J. Biochem. Biophys. 19, 320-323.
    • (1982) Ind. J. Biochem. Biophys. , vol.19 , pp. 320-323
    • Samanta, A.K.1    Bhaduri, A.2
  • 20
    • 0022978828 scopus 로고
    • UDP-galactose 4-epimerase from Saccharomyces fragilis: Presence of an essential arginine residue at the substrate binding site of the enzyme
    • Mukherjee, S. & Bhaduri, A. (1986) UDP-galactose 4-epimerase from Saccharomyces fragilis: Presence of an essential arginine residue at the substrate binding site of the enzyme, J. Biol. Chem. 261, 4519-4524.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4519-4524
    • Mukherjee, S.1    Bhaduri, A.2
  • 21
    • 0031053442 scopus 로고    scopus 로고
    • Reversible folding of UDP-galactose 4-epimerase from Esherichia coli
    • Dutta, S., Maity, N. R. & Bhattacharyya, D. (1997) Reversible folding of UDP-galactose 4-epimerase from Esherichia coli, Eur. J. Biochem. 244, 407-413.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 407-413
    • Dutta, S.1    Maity, N.R.2    Bhattacharyya, D.3
  • 22
    • 0000451294 scopus 로고
    • The enzymic interconversion of uridine diphospho-galactose and uridine diphospho-glucose
    • Maxell, H. S. (1957) The enzymic interconversion of uridine diphospho-galactose and uridine diphospho-glucose, J. Biol. Chem. 229, 139-151.
    • (1957) J. Biol. Chem. , vol.229 , pp. 139-151
    • Maxell, H.S.1
  • 23
    • 0016749444 scopus 로고
    • UDP-glucose 4-epimerase from Saccharomyces fragilis. Allosteric kinetics with UDP-glucose as substrate
    • Ray, M. & Bhaduri, A. (1975) UDP-glucose 4-epimerase from Saccharomyces fragilis. Allosteric kinetics with UDP-glucose as substrate, J. Biol. Chem. 250, 4373-4375.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4373-4375
    • Ray, M.1    Bhaduri, A.2
  • 24
    • 0025260865 scopus 로고
    • The mechanism of protein folding: Implications of in vitro refolding models for de novo protein folding and translocation in the cell
    • Fischer, G. & Schmid, F. X. (1990) The mechanism of protein folding: implications of in vitro refolding models for de novo protein folding and translocation in the cell, Biochemistry 29, 2205-2212.
    • (1990) Biochemistry , vol.29 , pp. 2205-2212
    • Fischer, G.1    Schmid, F.X.2
  • 25
    • 0001848681 scopus 로고
    • Folding of large proteins: Multidomain and multifunctional proteins
    • Creighton, T. E., ed. W. H. Freeman and Company, New York
    • Garel, J.-R. (1992) Folding of large proteins: Multidomain and multifunctional 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.