메뉴 건너뛰기




Volumn 270, Issue 23, 2003, Pages 4615-4627

A kinetic model of the branch-point between the methionine and threonine biosynthesis pathways in Arabidopsis thaliana

Author keywords

Allosteric activation; Branch point; Kinetic competition; Ping pong; Sensitivity coefficient

Indexed keywords

ADENOSINE PHOSPHATE; CYSTATHIONINE; CYSTATHIONINE GAMMA SYNTHASE; CYSTEINE; METHIONINE; PHOSPHATE; S ADENOSYLMETHIONINE; SERINE DERIVATIVE; SYNTHETASE; THREONINE; THREONINE SYNTHETASE; UNCLASSIFIED DRUG;

EID: 0345688035     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03851.x     Document Type: Article
Times cited : (51)

References (47)
  • 1
    • 0020649211 scopus 로고
    • The control of enzyme systems in vivo: Elasticity analysis of the steady state
    • Kacser, H. (1983) The control of enzyme systems in vivo: elasticity analysis of the steady state. Biochem. Soc. Trans. 11, 35-40.
    • (1983) Biochem. Soc. Trans. , vol.11 , pp. 35-40
    • Kacser, H.1
  • 2
    • 0021741048 scopus 로고
    • The branch point effect. Ultrasensitivity and subsensitivity to metabolic control
    • LaPorte, D.C., Walsh, K. & Koshland, D.E. (1984) The branch point effect. Ultrasensitivity and subsensitivity to metabolic control. J. Biol. Chem. 259, 14068-14075.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14068-14075
    • LaPorte, D.C.1    Walsh, K.2    Koshland, D.E.3
  • 3
    • 0025238865 scopus 로고
    • A 'top-down' approach to the determination of control coefficients in metabolic control theory
    • Brown, G.C., Hafner, R.P. & Brand, M.D. (1990) A 'top-down' approach to the determination of control coefficients in metabolic control theory. Eur. J. Biochem. 188, 321-325.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 321-325
    • Brown, G.C.1    Hafner, R.P.2    Brand, M.D.3
  • 4
    • 0021149774 scopus 로고
    • Determination of flux through the branch point of two metabolic cycles. The tricarboxylic acid cycle and the glyoxylate shunt
    • Walsh, K. & Koshland, D.E. (1984) Determination of flux through the branch point of two metabolic cycles. The tricarboxylic acid cycle and the glyoxylate shunt. J. Biol. Chem. 259, 9646-9654.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9646-9654
    • Walsh, K.1    Koshland, D.E.2
  • 5
    • 0021801376 scopus 로고
    • Branch point control by the phosphorylation state of isocitrate dehydrogenase. A quantitative examination of fluxes during a regulatory transition
    • Walsh, K. & Koshland, D.E. (1985) Branch point control by the phosphorylation state of isocitrate dehydrogenase. A quantitative examination of fluxes during a regulatory transition. J. Biol. Chem. 260, 8430-8437.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8430-8437
    • Walsh, K.1    Koshland, D.E.2
  • 6
    • 0033179481 scopus 로고    scopus 로고
    • Top-down control analysis of ATP turnover, glycolysis and oxidative phosphorylation in rat hepatocytes
    • Ainscow, E.K. & Brand, M.D. (1999) Top-down control analysis of ATP turnover, glycolysis and oxidative phosphorylation in rat hepatocytes. Eur. J. Biochem. 263, 671-685.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 671-685
    • Ainscow, E.K.1    Brand, M.D.2
  • 8
    • 0002672873 scopus 로고
    • Methionine biosynthesis in Enterobacteriaceae: Biochemical, regulatory, and evolutionary aspects
    • Saint-Girons, I., Parsot, C., Zakin, M.M., Barzu, O. & Cohen, G.N. (1988) Methionine biosynthesis in Enterobacteriaceae: biochemical, regulatory, and evolutionary aspects. CRC Crit. Rev. Biochem. 23, S1-S42.
    • (1988) CRC Crit. Rev. Biochem. , vol.23
    • Saint-Girons, I.1    Parsot, C.2    Zakin, M.M.3    Barzu, O.4    Cohen, G.N.5
  • 9
    • 0015979239 scopus 로고
    • Homocysteine biosynthesis in green plants. O-phosphorylhomoserine as the physiological substrate for cystathionine gamma-synthase
    • Datko, A.H., Giovanelli, J. & Mudd, S.H. (1974) Homocysteine biosynthesis in green plants. O-phosphorylhomoserine as the physiological substrate for cystathionine gamma-synthase. J. Biol. Chem. 249, 1139-1155.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1139-1155
    • Datko, A.H.1    Giovanelli, J.2    Mudd, S.H.3
  • 10
    • 0017183716 scopus 로고
    • Threonine synthase from higher plants: Stimulation by S-adenosylmethionine and inhibition by cysteine
    • Madison, J.T. & Thompson, G.H. (1976) Threonine synthase from higher plants: stimulation by S-adenosylmethionine and inhibition by cysteine. Biochem. Biophys. Res. Commun. 71, 684-691.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 684-691
    • Madison, J.T.1    Thompson, G.H.2
  • 11
    • 0000087176 scopus 로고
    • Intracellular localisation of aspartate kinase and the enzymes of threonine and methionine biosynthesis in green leaves
    • Wallsgrove, R.M., Lea, P.J. & Miflin, B.J. (1983) Intracellular localisation of aspartate kinase and the enzymes of threonine and methionine biosynthesis in green leaves. Plant Physiol. 71, 780-784.
    • (1983) Plant Physiol. , vol.71 , pp. 780-784
    • Wallsgrove, R.M.1    Lea, P.J.2    Miflin, B.J.3
  • 12
    • 0032522761 scopus 로고    scopus 로고
    • Cystathionine gamma-synthase from Arabidopsis thaliana: Purification and biochemical characterization of the recombinant enzyme over-expressed in Escherichia coli
    • Ravanel, S., Gakiere, B., Job, D. & Douce, R. (1998) Cystathionine gamma-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme over-expressed in Escherichia coli. Biochem. J. 331, 639-648.
    • (1998) Biochem. J. , vol.331 , pp. 639-648
    • Ravanel, S.1    Gakiere, B.2    Job, D.3    Douce, R.4
  • 14
    • 0030586270 scopus 로고    scopus 로고
    • Characterization of an Arabidopsis thaliana cDNA encoding an S-adenosylmethionine-sensitive threonine synthase. Threonine synthase from higher plants
    • Curien, G., Dumas, R., Ravanel, S. & Douce, R. (1996) Characterization of an Arabidopsis thaliana cDNA encoding an S-adenosylmethionine-sensitive threonine synthase. Threonine synthase from higher plants. FEBS Lett. 390, 85-90.
    • (1996) FEBS Lett. , vol.390 , pp. 85-90
    • Curien, G.1    Dumas, R.2    Ravanel, S.3    Douce, R.4
  • 15
    • 0032558460 scopus 로고    scopus 로고
    • Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine
    • Curien, G., Job, D., Douce, R. & Dumas, R. (1998) Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine. Biochemistry 37, 13212-13221.
    • (1998) Biochemistry , vol.37 , pp. 13212-13221
    • Curien, G.1    Job, D.2    Douce, R.3    Dumas, R.4
  • 17
    • 0002461993 scopus 로고
    • Effects of orthophosphate and adenosine 5′-phosphate on threonine synthase and cystathionine gamma-synthase of Lemna paucicostata Hegelm. 6746
    • Giovanelli, J., Mudd, S.H., Datko, A.H. & Thompson, G.H. (1986) Effects of orthophosphate and adenosine 5′-phosphate on threonine synthase and cystathionine gamma-synthase of Lemna paucicostata Hegelm. 6746. Plant Physiol. 81, 577-583.
    • (1986) Plant Physiol. , vol.81 , pp. 577-583
    • Giovanelli, J.1    Mudd, S.H.2    Datko, A.H.3    Thompson, G.H.4
  • 18
    • 0029854023 scopus 로고    scopus 로고
    • Purification and properties of cystathionine beta-lyase from Arabidopsis thaliana over-expressed in Escherichia coli
    • Ravanel, S., Job, D. & Douce, R. (1996) Purification and properties of cystathionine beta-lyase from Arabidopsis thaliana over-expressed in Escherichia coli. Biochem. J. 320, 383-392.
    • (1996) Biochem. J. , vol.320 , pp. 383-392
    • Ravanel, S.1    Job, D.2    Douce, R.3
  • 19
    • 0034642216 scopus 로고    scopus 로고
    • Evidence for two distinct effector-binding sites in threonine deaminase by site-directed mutagenesis, kinetic, and binding experiments
    • Wessel, P.M., Graciet, E., Douce, R. & Dumas, R. (2000) Evidence for two distinct effector-binding sites in threonine deaminase by site-directed mutagenesis, kinetic, and binding experiments. Biochemistry 39, 15136-15143.
    • (2000) Biochemistry , vol.39 , pp. 15136-15143
    • Wessel, P.M.1    Graciet, E.2    Douce, R.3    Dumas, R.4
  • 20
    • 0016160429 scopus 로고
    • Measurement of protein by spectroscopy at 205 nm
    • Scopes, R.K. (1974) Measurement of protein by spectroscopy at 205 nm. Anal. Biochem. 59, 277-282.
    • (1974) Anal. Biochem. , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 22
    • 0001296314 scopus 로고    scopus 로고
    • Transport, compartmentation, and metabolism of homoserine in higher plant cells. Carbon-13- and phosphorus-31-nuclear magnetic resonance studies carbon-13- and phosphorus-31-nuclear magnetic resonance studies
    • Aubert, S., Curien, G., Bligny, R., Gout, E. & Douce, R. (1998) Transport, compartmentation, and metabolism of homoserine in higher plant cells. Carbon-13-and phosphorus-31-nuclear magnetic resonance studies carbon-13-and phosphorus-31-nuclear magnetic resonance studies. Plant Physiol. 116, 547-557.
    • (1998) Plant Physiol. , vol.116 , pp. 547-557
    • Aubert, S.1    Curien, G.2    Bligny, R.3    Gout, E.4    Douce, R.5
  • 23
    • 0033736521 scopus 로고    scopus 로고
    • Mechanisms to account for maintenance of the soluble methionine pool in transgenic Arabidopsis plants expressing antisense cystathionine gamma-synthase cDNA
    • Gakiere, B., Ravanel, S., Droux, M., Douce, R. & Job, D. (2000) Mechanisms to account for maintenance of the soluble methionine pool in transgenic Arabidopsis plants expressing antisense cystathionine gamma-synthase cDNA. C. R. Acad. Sci. III 323, 841-851.
    • (2000) C. R. Acad. Sci. III , vol.323 , pp. 841-851
    • Gakiere, B.1    Ravanel, S.2    Droux, M.3    Douce, R.4    Job, D.5
  • 24
    • 0034126920 scopus 로고    scopus 로고
    • Mutation in the threonine synthase gene results in an over-accumulation of soluble methionine in Arabidopsis
    • Bartlem, D., Lambein, I., Okamoto, T., Itaya, A., Uda, Y., Kijima, F., Tamaki, Y., Nambara, E. & Naito, S. (2000) Mutation in the threonine synthase gene results in an over-accumulation of soluble methionine in Arabidopsis. Plant Physiol. 123, 101-110.
    • (2000) Plant Physiol. , vol.123 , pp. 101-110
    • Bartlem, D.1    Lambein, I.2    Okamoto, T.3    Itaya, A.4    Uda, Y.5    Kijima, F.6    Tamaki, Y.7    Nambara, E.8    Naito, S.9
  • 25
    • 0036008585 scopus 로고    scopus 로고
    • High free-methionine and decreased lignin content result from a mutation in the Arabidopsis S-adenosyl-L-methionine synthetase 3 gene
    • Shen, B., Li, C. & Tarczynski, M.C. (2002) High free-methionine and decreased lignin content result from a mutation in the Arabidopsis S-adenosyl-L-methionine synthetase 3 gene. Plant J. 29, 371-380.
    • (2002) Plant J. , vol.29 , pp. 371-380
    • Shen, B.1    Li, C.2    Tarczynski, M.C.3
  • 26
    • 0032483994 scopus 로고    scopus 로고
    • Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana
    • Noji, M., Inoue, K., Kimura, N., Gouda, A. & Saito, K. (1998) Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana. J. Biol. Chem. 273, 32739-32745.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32739-32745
    • Noji, M.1    Inoue, K.2    Kimura, N.3    Gouda, A.4    Saito, K.5
  • 28
    • 0028800634 scopus 로고
    • Methionine biosynthesis in higher plants. I. Purification and characterization of cystathionine gamma-synthase from spinach chloroplasts
    • Ravanel, S., Droux, M. & Douce, R. (1995) Methionine biosynthesis in higher plants. I. Purification and characterization of cystathionine gamma-synthase from spinach chloroplasts. Arch. Biochem. Biophys. 316, 572-584.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 572-584
    • Ravanel, S.1    Droux, M.2    Douce, R.3
  • 29
    • 77956845923 scopus 로고
    • Structure and function of the plastid envelope
    • Douce, R. & Joyard, J. (1979) Structure and function of the plastid envelope. Adv. Bot. Res. 7, 1-116.
    • (1979) Adv. Bot. Res. , vol.7 , pp. 1-116
    • Douce, R.1    Joyard, J.2
  • 30
    • 0009912615 scopus 로고
    • In vivo regulation of threonine and isoleucine biosynthesis in Lemna paucicostata Hegelm. 6746
    • Giovanelli, J., Mudd, S.H. & Datko, A.H. (1988) In vivo regulation of threonine and isoleucine biosynthesis in Lemna paucicostata Hegelm. 6746. Plant Physiol. 86, 369-377.
    • (1988) Plant Physiol. , vol.86 , pp. 369-377
    • Giovanelli, J.1    Mudd, S.H.2    Datko, A.H.3
  • 31
    • 0002325295 scopus 로고
    • Regulatory aspects of cysteine and methionine biosynthesis
    • Rennenberg, H., Brunold, C., DeDok, L.J. & Stulen, I., eds. SLDP Academic Public, The Hague
    • Giovanelli, J. (1990) Regulatory aspects of cysteine and methionine biosynthesis. In Sulfur Nutrition and Sulfur Assimilation in Higher Plants. (Rennenberg, H., Brunold, C., DeDok, L.J. & Stulen, I., eds), pp. 33-48. SLDP Academic Public, The Hague.
    • (1990) Sulfur Nutrition and Sulfur Assimilation in Higher Plants
    • Giovanelli, J.1
  • 32
    • 0011559120 scopus 로고
    • Responses of sulfur-containing compounds in Lemna paucicostata Hegelm. 6746 to changes in availability of sulfur sources
    • Datko, A.H. & Mudd, S.H. (1984) Responses of sulfur-containing compounds in Lemna paucicostata Hegelm. 6746 to changes in availability of sulfur sources. Plant Physiol. 75, 474-479.
    • (1984) Plant Physiol. , vol.75 , pp. 474-479
    • Datko, A.H.1    Mudd, S.H.2
  • 33
    • 0027976083 scopus 로고
    • Subcellular Volumes and metabolite concentrations in spinach leaves
    • Winter, H., Robinson, D.G. & Heldt, H.W. (1994) Subcellular Volumes and metabolite concentrations in spinach leaves. Planta 193, 530-535.
    • (1994) Planta , vol.193 , pp. 530-535
    • Winter, H.1    Robinson, D.G.2    Heldt, H.W.3
  • 34
    • 0000245049 scopus 로고
    • Adenine nucleotide levels in the cytosol, chloroplasts, and mitochondria of wheat leaf protoplasts
    • Stitt, M., Lilley, R.M.C. & Heldt, H.W. (1982) Adenine nucleotide levels in the cytosol, chloroplasts, and mitochondria of wheat leaf protoplasts. Plant Physiol. 70, 971-977.
    • (1982) Plant Physiol. , vol.70 , pp. 971-977
    • Stitt, M.1    Lilley, R.M.C.2    Heldt, H.W.3
  • 36
    • 0015949375 scopus 로고
    • A linear steady-state treatment of enzymatic chains. A mathematical model of glycolysis of human erythrocytes
    • Rapoport, T.A., Heinrich, R., Jacobasch, G. & Rapoport, S. (1974) A linear steady-state treatment of enzymatic chains. A mathematical model of glycolysis of human erythrocytes. Eur. J. Biochem. 42, 107-120.
    • (1974) Eur. J. Biochem. , vol.42 , pp. 107-120
    • Rapoport, T.A.1    Heinrich, R.2    Jacobasch, G.3    Rapoport, S.4
  • 37
    • 0000944264 scopus 로고
    • Metabolic control theory: Its role in microbiology and biotechnology
    • Kell, D. & Westerhoff, H.V. (1986) Metabolic control theory: its role in microbiology and biotechnology. FEMS Microbiol. Rev. 39, 305-320.
    • (1986) FEMS Microbiol. Rev. , vol.39 , pp. 305-320
    • Kell, D.1    Westerhoff, H.V.2
  • 38
    • 0026802334 scopus 로고
    • Metabolic control analysis: A survey of its theoretical and experimental development
    • Fell, D.A. (1992) Metabolic control analysis: a survey of its theoretical and experimental development. Biochem. J. 286 (2), 313-330.
    • (1992) Biochem. J. , vol.286 , Issue.2 , pp. 313-330
    • Fell, D.A.1
  • 41
    • 0019631384 scopus 로고
    • A generalized theory of the transition time for sequential enzyme reactions
    • Easterby, J.S. (1981) A generalized theory of the transition time for sequential enzyme reactions. Biochem. J. 199, 155-161.
    • (1981) Biochem. J. , vol.199 , pp. 155-161
    • Easterby, J.S.1
  • 42
    • 0018948321 scopus 로고
    • S-adenosylmethionine-a novel regulator of aspartate kinase
    • Rognes, S.E., Lea, P.J. & Miflin, B.J. (1980) S-adenosylmethionine-a novel regulator of aspartate kinase. Nature 287, 357-359.
    • (1980) Nature , vol.287 , pp. 357-359
    • Rognes, S.E.1    Lea, P.J.2    Miflin, B.J.3
  • 43
    • 0038475950 scopus 로고    scopus 로고
    • Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine
    • Paris, S., Viemon, C., Curien, G. & Dumas, R. (2003) Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine. J. Biol. Chem. 278, 5361-5366.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5361-5366
    • Paris, S.1    Viemon, C.2    Curien, G.3    Dumas, R.4
  • 45
    • 0034760328 scopus 로고    scopus 로고
    • The first exon coding region of cystathionine gamma-synthase gene is necessary and sufficient for down-regulation of its own mRNA accumulation in transgenic Arabidopsis thaliana
    • Suzuki, A., Shirata, Y., Ishida, H., Chiba, Y., Onouchi, H. & Naito, S. (2001) The first exon coding region of cystathionine gamma-synthase gene is necessary and sufficient for down-regulation of its own mRNA accumulation in transgenic Arabidopsis thaliana. Plant Cell Physiol. 42, 1174-1180.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 1174-1180
    • Suzuki, A.1    Shirata, Y.2    Ishida, H.3    Chiba, Y.4    Onouchi, H.5    Naito, S.6
  • 46
    • 85047681599 scopus 로고    scopus 로고
    • The N-terminal region of Arabidopsis cystathionine gamma-synthase plays an important regulatory role in methionine metabolism
    • Hacham, Y., Avraham, T. & Amir, R. (2002) The N-terminal region of Arabidopsis cystathionine gamma-synthase plays an important regulatory role in methionine metabolism. Plant Physiol. 128, 454-462.
    • (2002) Plant Physiol. , vol.128 , pp. 454-462
    • Hacham, Y.1    Avraham, T.2    Amir, R.3
  • 47
    • 0042838359 scopus 로고    scopus 로고
    • S-adenosyl-L-methionine is an effector in the posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis
    • Chiba, Y., Sakurai, R., Yoshino, M., Ominato, K., Ishikawa, M., Onouchi, H. & Naito, S. (2003) S-adenosyl-L-methionine is an effector in the posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis. Proc. Natl Acad. Sci. USA. 100, 10225-10230.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10225-10230
    • Chiba, Y.1    Sakurai, R.2    Yoshino, M.3    Ominato, K.4    Ishikawa, M.5    Onouchi, H.6    Naito, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.