메뉴 건너뛰기




Volumn 14, Issue 1, 1998, Pages 146-152

Overexpression of functional hydrolase domain of rat liver 10-formyltetrahydrofolate dehydrogenase in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

10 FORMYLTETRAHYDROFOLATE DEHYDROGENASE; ENZYME KINETICS; ENZYME PURIFICATION; HYDROLASE; ION EXCHANGE CHROMATOGRAPHY;

EID: 0032190003     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1998.0937     Document Type: Article
Times cited : (10)

References (27)
  • 1
    • 0022559134 scopus 로고
    • Purification of rat liver folate-binding protein: Cytosol I
    • Cook R. J., Wagner C. Purification of rat liver folate-binding protein: Cytosol I. Methods Enzymol. 122:1986;251-255.
    • (1986) Methods Enzymol. , vol.122 , pp. 251-255
    • Cook, R.J.1    Wagner, C.2
  • 2
    • 0027987995 scopus 로고
    • Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice
    • Champion K. M., Cook R. J., Tollaksen S. L., Giometti C. S. Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice. Proc. Natl. Acad. Sci. USA. 91:1994;11338-11342.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11338-11342
    • Champion, K.M.1    Cook, R.J.2    Tollaksen, S.L.3    Giometti, C.S.4
  • 3
    • 0001600926 scopus 로고
    • 10-Formyl tetrahydrofolate: NADP oxidoreductase
    • Kutzbach C., Stokstad E. L. R. 10-Formyl tetrahydrofolate: NADP oxidoreductase. Methods Enzymol. 18B:1971;793-798.
    • (1971) Methods Enzymol. , vol.18 , pp. 793-798
    • Kutzbach, C.1    Stokstad, E.L.R.2
  • 4
    • 0022545018 scopus 로고
    • Formyltetrahydrofolate dehydrogenase-hydrolase from pig liver: Simultaneous assay of the activities
    • Rios-Orlandi E. M., Zarkadas C. G., MacKenzie R. E. Formyltetrahydrofolate dehydrogenase-hydrolase from pig liver: Simultaneous assay of the activities. Biochim. Biophys. Acta. 87:1986;24-35.
    • (1986) Biochim. Biophys. Acta , vol.87 , pp. 24-35
    • Rios-Orlandi, E.M.1    Zarkadas, C.G.2    MacKenzie, R.E.3
  • 6
    • 0025828320 scopus 로고
    • Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase
    • Cook R. J., Lloyd R. S., Wagner C. Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase. J. Biol. Chem. 266:1991;4965-4973.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4965-4973
    • Cook, R.J.1    Lloyd, R.S.2    Wagner, C.3
  • 7
    • 0030942262 scopus 로고    scopus 로고
    • Domain structure of rat 10-formyltetrahydrofolate dehydrogenase. Resolution of the amino-terminal domain as 10-formyltetrahydrofolate hydrolase
    • Krupenko S. A., Wagner C., Cook R. J. Domain structure of rat 10-formyltetrahydrofolate dehydrogenase. Resolution of the amino-terminal domain as 10-formyltetrahydrofolate hydrolase. J. Biol. Chem. 272:1997;10273-10278.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10273-10278
    • Krupenko, S.A.1    Wagner, C.2    Cook, R.J.3
  • 8
    • 0030950437 scopus 로고    scopus 로고
    • Expression, purification, and properties of the aldehyde dehydrogenase homologous carboxyl-terminal domain of rat 10-formyltetrahydrofolate dehydrogenase
    • Krupenko S. A., Wagner C., Cook R. J. Expression, purification, and properties of the aldehyde dehydrogenase homologous carboxyl-terminal domain of rat 10-formyltetrahydrofolate dehydrogenase. J. Biol. Chem. 272:1997;10266-10272.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10266-10272
    • Krupenko, S.A.1    Wagner, C.2    Cook, R.J.3
  • 9
    • 0027525666 scopus 로고
    • Aldehyde dehydrogenases: Widespread structural and functional diversity within a shared framework
    • Hempel J., Nicholas H., Lindahl R. Aldehyde dehydrogenases: Widespread structural and functional diversity within a shared framework. Protein Sci. 2:1993;1890-1900.
    • (1993) Protein Sci. , vol.2 , pp. 1890-1900
    • Hempel, J.1    Nicholas, H.2    Lindahl, R.3
  • 10
    • 0025316947 scopus 로고
    • Active-site mapping and site-specific mutagenesis of glycinamide ribonucleotide transformylase fromEscherichia coli.
    • Inglese J., Smith J. M., Benkovic S. J. Active-site mapping and site-specific mutagenesis of glycinamide ribonucleotide transformylase fromEscherichia coli. Biochemistry. 29:1990;6678-6687.
    • (1990) Biochemistry , vol.29 , pp. 6678-6687
    • Inglese, J.1    Smith, J.M.2    Benkovic, S.J.3
  • 11
    • 0028923757 scopus 로고
    • Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts inEscherichia coli.
    • Nagy P. L., Marolewski A., Benkovic S. J., Zalkin H. Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts inEscherichia coli. J. Bacteriol. 177:1995;1292-1298.
    • (1995) J. Bacteriol. , vol.177 , pp. 1292-1298
    • Nagy, P.L.1    Marolewski, A.2    Benkovic, S.J.3    Zalkin, H.4
  • 13
    • 0029347159 scopus 로고
    • Baculovirus expression and purification of rat 10-formyltetrahydrofolate dehydrogenase
    • Krupenko S. A., Horstman D. A., Wagner C., Cook R. J. Baculovirus expression and purification of rat 10-formyltetrahydrofolate dehydrogenase. Protein Expression Purif. 6:1995;457-464.
    • (1995) Protein Expression Purif. , vol.6 , pp. 457-464
    • Krupenko, S.A.1    Horstman, D.A.2    Wagner, C.3    Cook, R.J.4
  • 15
    • 0001882924 scopus 로고
    • Inclusion bodies and recovery of proteins from the aggregated state
    • 20, Am. Chem. Soc. Washington, DC
    • De Bernardez-Clark, E. Georgiou, G. 1991, Inclusion bodies and recovery of proteins from the aggregated state, in, Protein Refolding, 1, 20, Am. Chem. Soc. Washington, DC.
    • (1991) In, Protein Refolding , pp. 1
    • De Bernardez-Clark, E.1    Georgiou, G.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0019551730 scopus 로고
    • "western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette W. N. "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:1981;195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 19
    • 0020794694 scopus 로고
    • Rapid and sensitive calorimetric method for visualizing biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: Bio-blots
    • Leary J. J., Brigati D. J., Ward D. C. Rapid and sensitive calorimetric method for visualizing biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: Bio-blots. Proc. Natl. Acad. Sci. USA. 80:1983;4045-4404.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4045-4404
    • Leary, J.J.1    Brigati, D.J.2    Ward, D.C.3
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 21
    • 0028911866 scopus 로고
    • Recombinant 10-formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate
    • Krupenko S. A., Wagner C., Cook R. J. Recombinant 10-formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate. Biochem. J. 306:1995;651-655.
    • (1995) Biochem. J. , vol.306 , pp. 651-655
    • Krupenko, S.A.1    Wagner, C.2    Cook, R.J.3
  • 22
    • 0019871881 scopus 로고
    • On the cofactor specificity of glycinamide ribonucleotide and 5-aminoimidazol-4-carboxamide ribonucleotide transformylase from chicken liver
    • Smith G. K., Mueller W. T., Benkovic P. A., Benkovic S. J. On the cofactor specificity of glycinamide ribonucleotide and 5-aminoimidazol-4-carboxamide ribonucleotide transformylase from chicken liver. Biochemistry. 20:1981;1241-1245.
    • (1981) Biochemistry , vol.20 , pp. 1241-1245
    • Smith, G.K.1    Mueller, W.T.2    Benkovic, P.A.3    Benkovic, S.J.4
  • 24
    • 0025365143 scopus 로고
    • Gene fusions for purpose of expression: An introduction
    • Uhlen M., Moks T. Gene fusions for purpose of expression: An introduction. Methods Enzymol. 185:1990;129-143.
    • (1990) Methods Enzymol. , vol.185 , pp. 129-143
    • Uhlen, M.1    Moks, T.2
  • 25
    • 0028061396 scopus 로고
    • Domain structure and function of 10-formyltetrahydrofolate dehydrogenase
    • Schirch D., Villar E., Maras B., Barra D., Schirch V. Domain structure and function of 10-formyltetrahydrofolate dehydrogenase. J. Biol. Chem. 269:1994;24728-24735.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24728-24735
    • Schirch, D.1    Villar, E.2    Maras, B.3    Barra, D.4    Schirch, V.5
  • 26
    • 0028938730 scopus 로고
    • Cysteine 707 is involved in the dehydrogenase active site of rat 10-formyltetrahydrofolate dehydrogenase
    • Krupenko S. A., Wagner C., Cook R. J. Cysteine 707 is involved in the dehydrogenase active site of rat 10-formyltetrahydrofolate dehydrogenase. J. Biol. Chem. 270:1995;519-522.
    • (1995) J. Biol. Chem. , vol.270 , pp. 519-522
    • Krupenko, S.A.1    Wagner, C.2    Cook, R.J.3
  • 27
    • 0031570328 scopus 로고    scopus 로고
    • Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion
    • Steinmetz C. G., Xie P., Weiner H., Hurley T. D. Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion. Structure. 5:1997;701-711.
    • (1997) Structure , vol.5 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.2    Weiner, H.3    Hurley, T.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.