메뉴 건너뛰기




Volumn 18, Issue 3, 2000, Pages 366-377

Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SYNTHESIS; AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SUBSTRATE; HIS7 GENE; HIS7 PROTEIN; HYBRID PROTEIN; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE; PROTEIN DOMAIN; PROTEIN EXPRESSION; STEADY STATE; X RAY CRYSTALLOGRAPHY;

EID: 0034089215     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1207     Document Type: Article
Times cited : (25)

References (31)
  • 1
    • 0029005482 scopus 로고
    • Evidence for cross-pathway regulation of metabolic gene expression in plants
    • Guyer D., Patton D., Ward E. Evidence for cross-pathway regulation of metabolic gene expression in plants. Proc. Natl. Acad. Sci. USA. 92:1995;4997-5000.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4997-5000
    • Guyer, D.1    Patton, D.2    Ward, E.3
  • 2
    • 0023896661 scopus 로고
    • Amino acid biosynthesis inhibitors as herbicides
    • Kishore G. M., Shah D. M. Amino acid biosynthesis inhibitors as herbicides. Annu. Rev. Biochem. 57:1988;627-663.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 627-663
    • Kishore, G.M.1    Shah, D.M.2
  • 4
    • 0013830963 scopus 로고
    • Mode of action of the herbicide, 3-amino-1,2,4-triazole (amitrole): Inhibition of an enzyme of histidine biosynthesis
    • Hilton J., Kearney P., Ames B. Mode of action of the herbicide, 3-amino-1,2,4-triazole (amitrole): Inhibition of an enzyme of histidine biosynthesis. Arch. Biochem. Biophys. 112:1965;544-547.
    • (1965) Arch. Biochem. Biophys. , vol.112 , pp. 544-547
    • Hilton, J.1    Kearney, P.2    Ames, B.3
  • 5
    • 0024279308 scopus 로고
    • Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons
    • Carlomagno M. S., Chiariotti L., Alifano P., Nappo A. G., Bruni C. B. Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons. J. Mol. Biol. 203:1988;585-606.
    • (1988) J. Mol. Biol. , vol.203 , pp. 585-606
    • Carlomagno, M.S.1    Chiariotti, L.2    Alifano, P.3    Nappo, A.G.4    Bruni, C.B.5
  • 6
    • 0020287279 scopus 로고
    • The nucleotide sequence of the HIS4 region of yeast
    • Donahue T. F., Farabaugh P. J., Fink G. R. The nucleotide sequence of the HIS4 region of yeast. Gene. 18:1982;47-59.
    • (1982) Gene , vol.18 , pp. 47-59
    • Donahue, T.F.1    Farabaugh, P.J.2    Fink, G.R.3
  • 8
    • 0000232594 scopus 로고    scopus 로고
    • Biosynthesis of histidine
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, & H. E. Umbarger. Washington: Am. Soc. Microbiol.
    • Winkler M. E. Biosynthesis of histidine. Neidhardt F. C., Ingraham J. L., Low K. B., Magasanik B., Schaechter M., Umbarger H. E. Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. 1996;485-505 Am. Soc. Microbiol. Washington.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 485-505
    • Winkler, M.E.1
  • 9
    • 0030612596 scopus 로고    scopus 로고
    • Evolutionary analysis of the hisCGABdFDEHI gene cluster from the archeon Sulfolobus solfataricus P2
    • Charlebois R. L., Sensen C. W., Doolittle W. F., Brown J. R. Evolutionary analysis of the hisCGABdFDEHI gene cluster from the archeon Sulfolobus solfataricus P2. J. Bacteriol. 179:1997;4429-4432.
    • (1997) J. Bacteriol. , vol.179 , pp. 4429-4432
    • Charlebois, R.L.1    Sensen, C.W.2    Doolittle, W.F.3    Brown, J.R.4
  • 10
    • 0028899164 scopus 로고
    • Purification and characterization of the imidazoleglycerol-phosphate dehydratase of Saccharomyces cerevisiae from recombinant Escherichia coli
    • Hawkes T. R., Thomas P. G., Edwards L. S., Rayner S. J., Wilkinson K. W., Rice D. W. Purification and characterization of the imidazoleglycerol-phosphate dehydratase of Saccharomyces cerevisiae from recombinant Escherichia coli. Biochem. J. 306:1995;385-397.
    • (1995) Biochem. J. , vol.306 , pp. 385-397
    • Hawkes, T.R.1    Thomas, P.G.2    Edwards, L.S.3    Rayner, S.J.4    Wilkinson, K.W.5    Rice, D.W.6
  • 11
    • 0027184407 scopus 로고
    • Gene inactivation in Lactococcus lactis: Histidine biosynthesis
    • Delorme C., Godon J. J., Ehrlich S. D., Renault P. Gene inactivation in Lactococcus lactis: Histidine biosynthesis. J. Bacteriol. 175:1993;4391-4399.
    • (1993) J. Bacteriol. , vol.175 , pp. 4391-4399
    • Delorme, C.1    Godon, J.J.2    Ehrlich, S.D.3    Renault, P.4
  • 12
    • 0028355575 scopus 로고
    • The evolution of the histidine biosynthetic genes in prokaryotes: A common ancestor for the hisA and hisF genes
    • Fani R., Lio P., Chiarelli I., Bazzicalupo M. The evolution of the histidine biosynthetic genes in prokaryotes: A common ancestor for the hisA and hisF genes. J. Mol. Evol. 38:1994;489-495.
    • (1994) J. Mol. Evol. , vol.38 , pp. 489-495
    • Fani, R.1    Lio, P.2    Chiarelli, I.3    Bazzicalupo, M.4
  • 14
    • 0027265544 scopus 로고
    • Cloning, primary structure, and regulation of the HIS7 gene encoding a bifunctional glutamine amidotransferase: Cyclase from Saccharomyces cerevisiae
    • Kuenzler M., Balmelli T., Egli C. M., Paravicini G., Braus G. H. Cloning, primary structure, and regulation of the HIS7 gene encoding a bifunctional glutamine amidotransferase: Cyclase from Saccharomyces cerevisiae. J. Bacteriol. 175:1993;5548-5558.
    • (1993) J. Bacteriol. , vol.175 , pp. 5548-5558
    • Kuenzler, M.1    Balmelli, T.2    Egli, C.M.3    Paravicini, G.4    Braus, G.H.5
  • 15
    • 0030957783 scopus 로고    scopus 로고
    • Structure of carbamoyl phosphate synthetase: A journey of 96 Å from substrate to product
    • Thoden J. B., Holden H. M., Wesenberg G., Raushel F. M., Rayment I. Structure of carbamoyl phosphate synthetase: A journey of 96 Å from substrate to product. Biochemistry. 36:1997;6305-6316.
    • (1997) Biochemistry , vol.36 , pp. 6305-6316
    • Thoden, J.B.1    Holden, H.M.2    Wesenberg, G.3    Raushel, F.M.4    Rayment, I.5
  • 16
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector
    • Furste J. P., Pansegrau W., Frank R. B. H., Scholz P. B. M., Lanka E. Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene. 48:1986;119-131.
    • (1986) Gene , vol.48 , pp. 119-131
    • Furste, J.P.1    Pansegrau, W.2    Frank, R.B.H.3    Scholz, P.B.M.4    Lanka, E.5
  • 20
    • 0027254139 scopus 로고
    • Imidazole glycerol phosphate synthase: The glutamine amidotransferase in histidine biosynthesis
    • Klem T. J., Davisson V. J. Imidazole glycerol phosphate synthase: The glutamine amidotransferase in histidine biosynthesis. Biochemistry. 32:1993;5177-5186.
    • (1993) Biochemistry , vol.32 , pp. 5177-5186
    • Klem, T.J.1    Davisson, V.J.2
  • 21
    • 0028205868 scopus 로고
    • A plasmid based approach for the synthesis of a histidine biosynthesis intermediate
    • Davisson V. J., Deras I. L., Hamilton S. E., Moore L. L. A plasmid based approach for the synthesis of a histidine biosynthesis intermediate. J. Org. Chem. 59:1994;137-143.
    • (1994) J. Org. Chem. , vol.59 , pp. 137-143
    • Davisson, V.J.1    Deras, I.L.2    Hamilton, S.E.3    Moore, L.L.4
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. 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.1
  • 30
    • 0032564321 scopus 로고    scopus 로고
    • Regulatory control of the amidotransferase domain of carbamoyl phosphate synthetase
    • Miles B. W., Banzon J. A., Raushel F. M. Regulatory control of the amidotransferase domain of carbamoyl phosphate synthetase. Biochemistry. 37:1998;16773-16779.
    • (1998) Biochemistry , vol.37 , pp. 16773-16779
    • Miles, B.W.1    Banzon, J.A.2    Raushel, F.M.3
  • 31
    • 0342894815 scopus 로고    scopus 로고
    • Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site
    • Krahn J. M., Kim J. H., Burns M. R., Parry R. J., Zalkin H., Smith J. L. Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Biochemistry. 36:1997;11061-11068.
    • (1997) Biochemistry , vol.36 , pp. 11061-11068
    • Krahn, J.M.1    Kim, J.H.2    Burns, M.R.3    Parry, R.J.4    Zalkin, H.5    Smith, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.