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Volumn 31, Issue 3, 1998, Pages 258-263

Functional amino acid residues of recombinant tobacco acetolactate synthase

Author keywords

5,5 Dithio bis (2 nitrobenzoic acid); Acetolactate synthase; N bromosuccinimide; N ethylmaleimide; Tobacco

Indexed keywords


EID: 0032395802     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (28)
  • 1
    • 84987057702 scopus 로고
    • Mode of action of herbicidal ALS-inhibitors on acetolactate synthase from green plant cell cultures, yeast, and Escherichia coli
    • Babczinski, P. and Zelinski, Z. (1991) Mode of action of herbicidal ALS-inhibitors on acetolactate synthase from green plant cell cultures, yeast, and Escherichia coli. Pestic. Sci. 31, 305-323.
    • (1991) Pestic. Sci. , vol.31 , pp. 305-323
    • Babczinski, P.1    Zelinski, Z.2
  • 2
    • 0023626886 scopus 로고
    • Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria
    • Barak, Z., Chipman, M. D., and Gollop, N. (1987) Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. J. Bacteriol. 169, 3750-3756.
    • (1987) J. Bacteriol. , vol.169 , pp. 3750-3756
    • Barak, Z.1    Chipman, M.D.2    Gollop, N.3
  • 3
    • 0029154215 scopus 로고
    • A naturally occurring point mutation confers broads range tolerance to herbicides that target acetolactate synthase
    • Bernasconi, P., Woodworth, A. R., Rosen, B. A., Subramanian, M. V., and Siehl, D. L. (1995) A naturally occurring point mutation confers broads range tolerance to herbicides that target acetolactate synthase. J. Biol. Chem. 270, 17381-17385.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17381-17385
    • Bernasconi, P.1    Woodworth, A.R.2    Rosen, B.A.3    Subramanian, M.V.4    Siehl, D.L.5
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0027144017 scopus 로고
    • Characterization of a novel form of thymidylate synthase: A heterodimer isolated after specific chemical modification of the immobilized native enzyme
    • Bradshaw, T. P. and Dunlap, R. B. (1993) Characterization of a novel form of thymidylate synthase: A heterodimer isolated after specific chemical modification of the immobilized native enzyme. Biochemistry 32, 12774-12781.
    • (1993) Biochemistry , vol.32 , pp. 12774-12781
    • Bradshaw, T.P.1    Dunlap, R.B.2
  • 6
    • 0031589993 scopus 로고    scopus 로고
    • Soluble overexpression in Escherichia coli, and purification and characterization of wild-type recombinant tobacco acetolactate synthase
    • Chang, S.-I., Kang, M-K., Choi, J. D., and Namgoong, S. K. (1997) Soluble overexpression in Escherichia coli, and purification and characterization of wild-type recombinant tobacco acetolactate synthase. Biochem Biophy. Res. Comm. 234, 549-553.
    • (1997) Biochem Biophy. Res. Comm. , vol.234 , pp. 549-553
    • Chang, S.-I.1    Kang, M.-K.2    Choi, J.D.3    Namgoong, S.K.4
  • 7
    • 0019890805 scopus 로고
    • Roles of arginyl residues in pyridoxamine-5-phosphate oxidase from rabbit liver
    • Choi, J. D. and McCormick, D. B. (1981) Roles of arginyl residues in pyridoxamine-5-phosphate oxidase from rabbit liver. Biochemistry 20, 5272-5278.
    • (1981) Biochemistry , vol.20 , pp. 5272-5278
    • Choi, J.D.1    McCormick, D.B.2
  • 8
    • 0011184097 scopus 로고
    • Inhibition of acetolactate synthase by pyrimidyl-oxybenzoate and pyrimidyl-thio-benzoate
    • presently J. Biochem. Mol. Biol.
    • Choi, J. D., Moon, Y., Chang, S.-I., Chae, J. K., and Shin, J. H. (1993) Inhibition of acetolactate synthase by pyrimidyl-oxybenzoate and pyrimidyl-thio-benzoate. Korean Biochem. J. (presently J. Biochem. Mol. Biol.) 26, 638-643.
    • (1993) Korean Biochem. J. , vol.26 , pp. 638-643
    • Choi, J.D.1    Moon, Y.2    Chang, S.-I.3    Chae, J.K.4    Shin, J.H.5
  • 9
    • 0031530056 scopus 로고    scopus 로고
    • Purification and characterization of acetolactate synthase from barley
    • formerly Korean Biochem. J.
    • Chong, C. K., Chang, S.-I., and Choi, J. D. (1997) Purification and characterization of acetolactate synthase from barley. J. Biochem. Mol. Biol. (formerly Korean Biochem. J.) 30, 274-279.
    • (1997) J. Biochem. Mol. Biol. , vol.30 , pp. 274-279
    • Chong, C.K.1    Chang, S.-I.2    Choi, J.D.3
  • 10
    • 0017816893 scopus 로고
    • A comparative study of the acetohydroxy acid synthase isozyme of Escherichia coli K-12
    • De Felice, M. J., Squires, C. H., and Levinthal, M. (1978) A comparative study of the acetohydroxy acid synthase isozyme of Escherichia coli K-12. Biochem. Biophys. Acta. 541, 9-17.
    • (1978) Biochem. Biophys. Acta , vol.541 , pp. 9-17
    • De Felice, M.J.1    Squires, C.H.2    Levinthal, M.3
  • 11
  • 12
    • 0021352116 scopus 로고
    • Purification and subunit composition of acetohydroxy acid synthase I from Escherichia coli K-12
    • Eoyang, L. and Silverman, P. M. (1984) Purification and subunit composition of acetohydroxy acid synthase I from Escherichia coli K-12. J. Bacteriol. 157, 184-189.
    • (1984) J. Bacteriol. , vol.157 , pp. 184-189
    • Eoyang, L.1    Silverman, P.M.2
  • 13
    • 3043000209 scopus 로고
    • Inhibition of acetohydroxy acid synthase by leucine
    • Gollop, N., Chipman, D. M., and Barak, B. C. (1983) Inhibition of acetohydroxy acid synthase by leucine. Biochem. Biophys. Acta. 541, 1-9.
    • (1983) Biochem. Biophys. Acta , vol.541 , pp. 1-9
    • Gollop, N.1    Chipman, D.M.2    Barak, B.C.3
  • 14
    • 0030468649 scopus 로고    scopus 로고
    • Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis
    • Ibdah, M., Ilan, A. B., Livnah, O. L., Schloss, J. V., Barak, Z., and Chipman, D. M. (1996) Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis. Biochemistry 35, 16282-16291.
    • (1996) Biochemistry , vol.35 , pp. 16282-16291
    • Ibdah, M.1    Ilan, A.B.2    Livnah, O.L.3    Schloss, J.V.4    Barak, Z.5    Chipman, D.M.6
  • 16
    • 0021195869 scopus 로고
    • Herbicide-resistant mutants from tobacco cell cultures
    • LaRossa, R. A. and Schloss, J. V. (1984) Herbicide-resistant mutants from tobacco cell cultures. J. Biol. Chem. 259, 8753-8757.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8753-8757
    • LaRossa, R.A.1    Schloss, J.V.2
  • 17
    • 0001544805 scopus 로고
    • The development of herbicide resistant crops
    • Mazur, B. J. and Falco, S. C. (1989) The development of herbicide resistant crops. Annu. Rev. Plant Physiol. 40, 441-470.
    • (1989) Annu. Rev. Plant Physiol. , vol.40 , pp. 441-470
    • Mazur, B.J.1    Falco, S.C.2
  • 18
    • 0000809368 scopus 로고
    • The control of leucine, isoleucine and valine biosynthesis in a range of higher plants
    • Miflin, B. J. and Cave, P. R. (1972) The control of leucine, isoleucine and valine biosynthesis in a range of higher plants. J. Exp. Bot. 23, 511-516.
    • (1972) J. Exp. Bot. , vol.23 , pp. 511-516
    • Miflin, B.J.1    Cave, P.R.2
  • 19
    • 0019877113 scopus 로고
    • Rat liver phenylalanine hydroxylase activation by sulfhydryl modification
    • Parniak, M. A. and Kaufman, S. (1981) Rat liver phenylalanine hydroxylase activation by sulfhydryl modification. J. Biol. Chem. 256, 6876-6882.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6876-6882
    • Parniak, M.A.1    Kaufman, S.2
  • 20
    • 0001476338 scopus 로고
    • Site of action of chlorsulfuron: Inhibition of valine and isoleucine biosynthesis in plants
    • Ray, T. B. (1984) Site of action of chlorsulfuron: Inhibition of valine and isoleucine biosynthesis in plants. Plant Physiol. 75, 827-831.
    • (1984) Plant Physiol. , vol.75 , pp. 827-831
    • Ray, T.B.1
  • 21
    • 0022356249 scopus 로고
    • Purification and properties of Salmonella typhimurium acetolactate synthase II from E. coli HB 101/pDU9
    • Schloss, J. V., Van Dyk, D. E., Vasta, J. F., and Kutny, R. M. (1985) Purification and properties of Salmonella typhimurium acetolactate synthase II from E. coli HB 101/pDU9. Biochemistry 24, 4952-4959.
    • (1985) Biochemistry , vol.24 , pp. 4952-4959
    • Schloss, J.V.1    Van Dyk, D.E.2    Vasta, J.F.3    Kutny, R.M.4
  • 22
    • 84957869700 scopus 로고
    • Physiological responses of corn (Zea mays) to ARSENAL herbicide
    • Shaner, D. L., Anderson, P. C., and Stidham, M. A. (1984) Physiological responses of corn (Zea mays) to ARSENAL herbicide. Plant Physiol. 76, 545-546.
    • (1984) Plant Physiol. , vol.76 , pp. 545-546
    • Shaner, D.L.1    Anderson, P.C.2    Stidham, M.A.3
  • 23
    • 21844490659 scopus 로고
    • The interaction of barley acetolactate synthase with 4,6-dimethoxypyrimidine inhibitors
    • formerly Korean Biochem. J.
    • Shim, H. O., Kim, D. W., Chang, S.-I., and Choi, J. D. (1995) The interaction of barley acetolactate synthase with 4,6-dimethoxypyrimidine inhibitors. J. Biochem. Mol. Biol. (formerly Korean Biochem. J.) 28, 471-476.
    • (1995) J. Biochem. Mol. Biol. , vol.28 , pp. 471-476
    • Shim, H.O.1    Kim, D.W.2    Chang, S.-I.3    Choi, J.D.4
  • 24
    • 0025876035 scopus 로고
    • Rat liver guanidinoacetate methyltransferase
    • Takata, Y., Date, T., and Fujioka, M. (1991) Rat liver guanidinoacetate methyltransferase. Biochem. J. 277, 399-406.
    • (1991) Biochem. J. , vol.277 , pp. 399-406
    • Takata, Y.1    Date, T.2    Fujioka, M.3
  • 25
    • 0001348712 scopus 로고
    • Biosynthesis of branched chain amino acids
    • F. C. Neidhardt, J. L., Ingraham, K. B., Low, K., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds.), American Society for Microbiology, Washington, DC
    • Umbarger, H. E. (1987) Biosynthesis of branched chain amino acids; in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, F. C. Neidhardt, J. L., Ingraham, K. B., Low, K., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds.), pp. 352-367, American Society for Microbiology, Washington, DC.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 352-367
    • Umbarger, H.E.1
  • 26
    • 84864301531 scopus 로고
    • A colorimetirc determination of blood acetoin
    • Westerfeld, W. W. (1943) A colorimetirc determination of blood acetoin. J. Biol. Chem. 161, 495-502.
    • (1943) J. Biol. Chem. , vol.161 , pp. 495-502
    • Westerfeld, W.W.1
  • 27
    • 0025173057 scopus 로고
    • Specific truncations of an acetolactate synthase gene from Brassica napus efficiently complement ilvB/ilvG mutants of Salmonella typhimurium
    • Wiersma, P. A., Hachey, J. E., Crosby, W. L., and Moloney, M. M. (1990) Specific truncations of an acetolactate synthase gene from Brassica napus efficiently complement ilvB/ilvG mutants of Salmonella typhimurium. Mol. Gen. Genet. 224, 155-159.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 155-159
    • Wiersma, P.A.1    Hachey, J.E.2    Crosby, W.L.3    Moloney, M.M.4
  • 28
    • 0027429696 scopus 로고
    • The role of cysteine residues 129 and 329 in Escherichia coli K1 CMP-NeuAc synthase
    • Zapata, G., Roller, P. P., Crowley, J., and Vann, W. F. (1993) The role of cysteine residues 129 and 329 in Escherichia coli K1 CMP-NeuAc synthase. Biochem. J. 295, 485-491.
    • (1993) Biochem. J. , vol.295 , pp. 485-491
    • Zapata, G.1    Roller, P.P.2    Crowley, J.3    Vann, W.F.4


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