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Volumn 47, Issue 45, 2008, Pages 11783-11792

Allosteric regulation of Bacillus subtilis threonine deaminase, a biosynthetic threonine deaminase with a single regulatory domain

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; BINDING SITES; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; ESCHERICHIA COLI; PLANTS (BOTANY); WATER POLLUTION;

EID: 55849117742     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800901n     Document Type: Article
Times cited : (23)

References (38)
  • 1
    • 0242577550 scopus 로고    scopus 로고
    • Beginnings of feedback inhibition, allostery, and multi-protein complexes
    • Pardee, A. B., and Reddy, G. P. (2003) Beginnings of feedback inhibition, allostery, and multi-protein complexes. Gene 321, 17-23.
    • (2003) Gene , vol.321 , pp. 17-23
    • Pardee, A.B.1    Reddy, G.P.2
  • 2
    • 0027665006 scopus 로고
    • Allosteric proteins: From regulatory enzymes to receptors-personal recollections
    • Changeux, J. P. (1993) Allosteric proteins: From regulatory enzymes to receptors-personal recollections. BioEssays 15, 625-634.
    • (1993) BioEssays , vol.15 , pp. 625-634
    • Changeux, J.P.1
  • 3
    • 0026936822 scopus 로고
    • The origin of a useful concept - feedback inhibition
    • Umbarger, H. E. (1992) The origin of a useful concept - feedback inhibition. Protein Sci. 1, 1392-1395.
    • (1992) Protein Sci , vol.1 , pp. 1392-1395
    • Umbarger, H.E.1
  • 4
    • 1542379833 scopus 로고    scopus 로고
    • Local and global control mechanisms in allosteric threonine deaminase
    • Gallagher, D. T., Chinchilla, D., Lau, H., and Eisenstein, E. (2004) Local and global control mechanisms in allosteric threonine deaminase. Methods Enzymol. 380, 85-106.
    • (2004) Methods Enzymol , vol.380 , pp. 85-106
    • Gallagher, D.T.1    Chinchilla, D.2    Lau, H.3    Eisenstein, E.4
  • 5
    • 0002546877 scopus 로고
    • The study of branched chain amino acid biosynthesis: Its roots and its fruits
    • Barak, Z, Chipman, D. M, and Schloss, J. V, Eds, pp, VCH, Weinheim, Germany
    • Umbarger, H. E. (1990) The study of branched chain amino acid biosynthesis: Its roots and its fruits, in Biosynthesis of Branched Chain Amino Acids (Barak, Z., Chipman, D. M., and Schloss, J. V., Eds.) pp 1-24, VCH, Weinheim, Germany.
    • (1990) Biosynthesis of Branched Chain Amino Acids , pp. 1-24
    • Umbarger, H.E.1
  • 6
    • 73049119821 scopus 로고
    • The feedback control mechanism of biosynthetic L-threonine deaminase by L-isoleucine
    • Changeux, J. P. (1961) The feedback control mechanism of biosynthetic L-threonine deaminase by L-isoleucine. Cold Spring Harbor Symp. Quant. Biol. 26, 313-330.
    • (1961) Cold Spring Harbor Symp. Quant. Biol , vol.26 , pp. 313-330
    • Changeux, J.P.1
  • 7
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J.-P. (1965) On the nature of allosteric transitions: A plausible model. J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 8
    • 0015219601 scopus 로고
    • Threonine deaminases from Saccharomyces cerevisiae mutationally altered in regulatory properties
    • Betz, J. L., Hereford, L. M., and Magee, P. T. (1971) Threonine deaminases from Saccharomyces cerevisiae mutationally altered in regulatory properties. Biochemistry 10, 1818-1824.
    • (1971) Biochemistry , vol.10 , pp. 1818-1824
    • Betz, J.L.1    Hereford, L.M.2    Magee, P.T.3
  • 9
    • 0013881090 scopus 로고
    • The allosteric threonine deaminase of Salmonella. Kinetic model for the native enzyme
    • Maeba, P., and Sanwal, B. D. (1966) The allosteric threonine deaminase of Salmonella. Kinetic model for the native enzyme. Biochemistry 5, 525-536.
    • (1966) Biochemistry , vol.5 , pp. 525-536
    • Maeba, P.1    Sanwal, B.D.2
  • 10
    • 0014408290 scopus 로고
    • Threonine deaminase from Salmonella typhimurium. II. The subunit structure
    • Zarlengo, M. H., Robinson, G. W., and Burns, R. O. (1968) Threonine deaminase from Salmonella typhimurium. II. The subunit structure. J. Biol. Chem. 243, 186-191.
    • (1968) J. Biol. Chem , vol.243 , pp. 186-191
    • Zarlengo, M.H.1    Robinson, G.W.2    Burns, R.O.3
  • 11
    • 0015877040 scopus 로고
    • Threonine deaminase from Escherichia coli. I. Purification and properties
    • Calhoun, D. H., Rimerman, R. A., and Hatfield, G. W. (1973) Threonine deaminase from Escherichia coli. I. Purification and properties. J. Biol. Chem. 248, 3511-3516.
    • (1973) J. Biol. Chem , vol.248 , pp. 3511-3516
    • Calhoun, D.H.1    Rimerman, R.A.2    Hatfield, G.W.3
  • 12
    • 0016630102 scopus 로고
    • Threonine deaminase from Salmonella typhimurium. Relationship between regulatory sites
    • Decedue, C. J., Hofler, J. G., and Burns, R. O. (1975) Threonine deaminase from Salmonella typhimurium. Relationship between regulatory sites. J. Biol. Chem. 250, 1563-1570.
    • (1975) J. Biol. Chem , vol.250 , pp. 1563-1570
    • Decedue, C.J.1    Hofler, J.G.2    Burns, R.O.3
  • 13
    • 0026095288 scopus 로고    scopus 로고
    • Eisenstein, E. (1991) Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli. J. Biol. Chem. 266, 5801-5807.
    • Eisenstein, E. (1991) Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli. J. Biol. Chem. 266, 5801-5807.
  • 14
    • 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., and 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
  • 15
    • 0014939369 scopus 로고
    • Threonine deaminase from Bacillus subtilis. II. The steady state kinetic properties
    • Hatfield, G. W., and Umbarger, H. E. (1970) Threonine deaminase from Bacillus subtilis. II. The steady state kinetic properties. J. Biol. Chem. 245, 1742-1747.
    • (1970) J. Biol. Chem , vol.245 , pp. 1742-1747
    • Hatfield, G.W.1    Umbarger, H.E.2
  • 16
    • 0028072488 scopus 로고
    • Energetics of cooperative ligand binding to the active sites of threonine deaminase
    • Eisenstein, E. (1994) Energetics of cooperative ligand binding to the active sites of threonine deaminase. J. Biol. Chem. 269, 29416-29422.
    • (1994) J. Biol. Chem , vol.269 , pp. 29416-29422
    • Eisenstein, E.1
  • 17
    • 0029089644 scopus 로고
    • An expanded two-state model accounts for homotropic cooperativity in biosynthetic threonine deaminase from Escherichia coli
    • Eisenstein, E., Yu, H. D., Fisher, K. E., Iacuzio, D. A., Ducote, K. R., and Schwarz, F. P. (1995) An expanded two-state model accounts for homotropic cooperativity in biosynthetic threonine deaminase from Escherichia coli. Biochemistry 34, 9403-9412.
    • (1995) Biochemistry , vol.34 , pp. 9403-9412
    • Eisenstein, E.1    Yu, H.D.2    Fisher, K.E.3    Iacuzio, D.A.4    Ducote, K.R.5    Schwarz, F.P.6
  • 18
    • 0028097441 scopus 로고
    • Cooperative binding of the feedback modifiers isoleucine and valine to threonine deaminase
    • Eisenstein, E., Yu, H. D., and Schwarz, F. P. (1994) Cooperative binding of the feedback modifiers isoleucine and valine to threonine deaminase. J. Biol. Chem. 269, 29423-29429.
    • (1994) J. Biol. Chem , vol.269 , pp. 29423-29429
    • Eisenstein, E.1    Yu, H.D.2    Schwarz, F.P.3
  • 19
    • 0032483527 scopus 로고    scopus 로고
    • Amino acid substitutions in the C-terminal regulatory domain disrupt allosteric effector binding to biosynthetic threonine deaminase from Escherichia coli
    • Chinchilla, D., Schwarz, F. P., and Eisenstein, E. (1998) Amino acid substitutions in the C-terminal regulatory domain disrupt allosteric effector binding to biosynthetic threonine deaminase from Escherichia coli. J. Biol. Chem. 273, 23219-23224.
    • (1998) J. Biol. Chem , vol.273 , pp. 23219-23224
    • Chinchilla, D.1    Schwarz, F.P.2    Eisenstein, E.3
  • 23
    • 0028804507 scopus 로고
    • Allosteric regulation of biosynthetic threonine deaminase from Escherichia coli: Effects of isoleucine and valine on active-site ligand binding and catalysis
    • Eisenstein, E. (1995) Allosteric regulation of biosynthetic threonine deaminase from Escherichia coli: Effects of isoleucine and valine on active-site ligand binding and catalysis. Arch. Biochem. Biophys. 316, 311-318.
    • (1995) Arch. Biochem. Biophys , vol.316 , pp. 311-318
    • Eisenstein, E.1
  • 24
    • 12744278334 scopus 로고    scopus 로고
    • A site-directed mutagenesis interrogation of the carboxy-terminal end of Arabidopsis thaliana threonine dehydratase/deaminase reveals a synergistic interaction between two effector-binding sites and contributes to the development of a novel selectable marker
    • Garcia, E. L., and Mourad, G. S. (2004) A site-directed mutagenesis interrogation of the carboxy-terminal end of Arabidopsis thaliana threonine dehydratase/deaminase reveals a synergistic interaction between two effector-binding sites and contributes to the development of a novel selectable marker. Plant Mol. Biol. 55, 121-134.
    • (2004) Plant Mol. Biol , vol.55 , pp. 121-134
    • Garcia, E.L.1    Mourad, G.S.2
  • 25
    • 2642521392 scopus 로고    scopus 로고
    • Role of a conserved arginine in the mechanism of acetohydroxyacid synthase: Catalysis of condensation with a specific ketoacid substrate
    • Engel, S., Vyazmensky, M., Vinogradov, M., Berkovich, D., BarIlan, A., Qimron, U., Rosiansky, Y., Barak, Z., and Chipman, D. M. (2004) Role of a conserved arginine in the mechanism of acetohydroxyacid synthase: Catalysis of condensation with a specific ketoacid substrate. J. Biol. Chem. 279, 24803-24812.
    • (2004) J. Biol. Chem , vol.279 , pp. 24803-24812
    • Engel, S.1    Vyazmensky, M.2    Vinogradov, M.3    Berkovich, D.4    BarIlan, A.5    Qimron, U.6    Rosiansky, Y.7    Barak, Z.8    Chipman, D.M.9
  • 26
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 27
    • 0014939333 scopus 로고
    • Threonine deaminase from Bacillus subtilis. I. Purification of the enzyme
    • Hatfield, G. W., and Umbarger, H. E. (1970) Threonine deaminase from Bacillus subtilis. I. Purification of the enzyme. J. Biol. Chem. 245, 1736-1741.
    • (1970) J. Biol. Chem , vol.245 , pp. 1736-1741
    • Hatfield, G.W.1    Umbarger, H.E.2
  • 28
    • 0017368370 scopus 로고
    • Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase
    • Penefsky, H. S. (1977) Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase. J. Biol. Chem. 252, 2891-2899.
    • (1977) J. Biol. Chem , vol.252 , pp. 2891-2899
    • Penefsky, H.S.1
  • 29
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of heamoglobin on its oxygen dissociation curve
    • Hill, A. V. (1910) The possible effects of the aggregation of the molecules of heamoglobin on its oxygen dissociation curve. J. Physiol. (Oxford, U.K.) 40, IV-VII.
    • (1910) J. Physiol. (Oxford, U.K.) , vol.40
    • Hill, A.V.1
  • 31
    • 0028141650 scopus 로고
    • Threonine dehydratases of Corynebacterium glutamicum with altered allosteric control: Their generation and biochemical and structural analysis
    • Mockel, B., Eggeling, L., and Sahm, H. (1994) Threonine dehydratases of Corynebacterium glutamicum with altered allosteric control: Their generation and biochemical and structural analysis. Mol. Microbiol. 13, 833-842.
    • (1994) Mol. Microbiol , vol.13 , pp. 833-842
    • Mockel, B.1    Eggeling, L.2    Sahm, H.3
  • 32
    • 0014014862 scopus 로고
    • On the nature of allosteric transitions: Implications of non-exclusive ligand binding
    • Rubin, M. M., and Changeux, J. P. (1966) On the nature of allosteric transitions: Implications of non-exclusive ligand binding. J. Mol. Biol. 21, 265-274.
    • (1966) J. Mol. Biol , vol.21 , pp. 265-274
    • Rubin, M.M.1    Changeux, J.P.2
  • 33
    • 0000572386 scopus 로고
    • Effect of the feedback inhibitor, CTP, on subunit interactions of aspartic transcarbamylase
    • Gerhart, J. C., and Pardee, A. B. (1963) Effect of the feedback inhibitor, CTP, on subunit interactions of aspartic transcarbamylase. Cold Spring Harbor Symp. Quant. Biol. 28, 491-496.
    • (1963) Cold Spring Harbor Symp. Quant. Biol , vol.28 , pp. 491-496
    • Gerhart, J.C.1    Pardee, A.B.2
  • 35
    • 0023267311 scopus 로고
    • Toxic accumulation of α-ketobutyrate caused by inhibition of the branched-chain amino acid biosynthetic enzyme acetolactate synthase in Salmonella typhimurium
    • LaRossa, R. A., VanDyk, T. K., and Smulski, D. R. (1987) Toxic accumulation of α-ketobutyrate caused by inhibition of the branched-chain amino acid biosynthetic enzyme acetolactate synthase in Salmonella typhimurium. J. Bacteriol. 169, 1372-1378.
    • (1987) J. Bacteriol , vol.169 , pp. 1372-1378
    • LaRossa, R.A.1    VanDyk, T.K.2    Smulski, D.R.3
  • 36
    • 0018379935 scopus 로고
    • Inhibition of Bacillus subtilis growth and sporulation by threonine
    • Lamb, D. H., and Bott, K. F. (1979) Inhibition of Bacillus subtilis growth and sporulation by threonine. J. Bacteriol. 137, 213-220.
    • (1979) J. Bacteriol , vol.137 , pp. 213-220
    • Lamb, D.H.1    Bott, K.F.2
  • 38
    • 38549141229 scopus 로고    scopus 로고
    • Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre
    • Bennett-Lovsey, R. M., Herbert, A. D., Sternberg, M. J., and Kelley, L. A. (2008) Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. Proteins 70, 611-625.
    • (2008) Proteins , vol.70 , pp. 611-625
    • Bennett-Lovsey, R.M.1    Herbert, A.D.2    Sternberg, M.J.3    Kelley, L.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.