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Gene Review

ECs3997  -  threonine dehydratase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs3997


High impact information on ECs3997


Chemical compound and disease context of ECs3997


Biological context of ECs3997


Associations of ECs3997 with chemical compounds

  • To a first approximation, the data are consistent with isoleucine and valine regulating threonine deaminase by shifting the allosteric equilibrium between the different affinity forms [8].
  • The catalytic activity of threonine deaminase is absolutely dependent on the presence of pyridoxal phosphate, and the tetrameric molecule is isolated containing 1 mol of cofactor/56,000-Da chain [1].
  • Wild-type threonine deaminase demonstrates a sigmoidal dependence of initial velocity on threonine concentration in the absence of isoleucine, consistent with a substrate-promoted conversion of the enzyme from a low activity to a high activity conformation [1].
  • Both 2-aminobutyrate and alanine bind cooperatively to four sites on threonine deaminase, with an average dissociation constant of 12.7 and 43.8 mM, respectively [8].
  • Valine treatment of nonstarved or methionine-starved cells led to the expected increase in threonine deaminase and transaminase B activities [14].

Analytical, diagnostic and therapeutic context of ECs3997


  1. Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli. Eisenstein, E. J. Biol. Chem. (1991) [Pubmed]
  2. Homocysteine toxicity in Escherichia coli is caused by a perturbation of branched-chain amino acid biosynthesis. Tuite, N.L., Fraser, K.R., O'byrne, C.P. J. Bacteriol. (2005) [Pubmed]
  3. Crystallization and preliminary X-ray crystallographic analysis of biodegradative threonine deaminase (TdcB) from Salmonella typhimurium. Simanshu, D.K., Chittori, S., Savithri, H.S., Murthy, M.R. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
  4. Crystal Structures of Salmonella typhimurium Biodegradative Threonine Deaminase and Its Complex with CMP Provide Structural Insights into Ligand-induced Oligomerization and Enzyme Activation. Simanshu, D.K., Savithri, H.S., Murthy, M.R. J. Biol. Chem. (2006) [Pubmed]
  5. Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to D-cysteine. Soutourina, J., Blanquet, S., Plateau, P. J. Biol. Chem. (2001) [Pubmed]
  6. 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., Eisenstein, E. J. Biol. Chem. (1998) [Pubmed]
  7. Cooperative binding of the feedback modifiers isoleucine and valine to biosynthetic threonine deaminase from Escherichia coli. Eisenstein, E., Yu, H.D., Schwarz, F.P. J. Biol. Chem. (1994) [Pubmed]
  8. Energetics of cooperative ligand binding to the active sites of biosynthetic threonine deaminase from Escherichia coli. Eisenstein, E. J. Biol. Chem. (1994) [Pubmed]
  9. Cysteine and growth inhibition of Escherichia coli: threonine deaminase as the target enzyme. Harris, C.L. J. Bacteriol. (1981) [Pubmed]
  10. Threonine deaminase from a nonsense mutant of Escherichia coli requiring isoleucine or pyridoxine: evidence for half-of-the-sites reactivity. Feldner, J., Grimminger, H. J. Bacteriol. (1976) [Pubmed]
  11. Threonine deaminase from Escherichia coli. II. Maturation and physical properties of the enzyme from a mutant altered in its regulation of gene expression. Calhoun, D.H., Kuska, J.S., Hatfield, G.W. J. Biol. Chem. (1975) [Pubmed]
  12. The regulation of the ilv ADGE operon: evidence for positive control by threonine deaminase. Levinthal, M., Levinthal, M., Williams, L.S. J. Mol. Biol. (1976) [Pubmed]
  13. Role of threonine dehydrogenase in Escherichia coli threonine degradation. Potter, R., Kapoor, V., Newman, E.B. J. Bacteriol. (1977) [Pubmed]
  14. Cysteine starvation, isoleucyl-tRNAIle, and the regulation of the ilvGEDA operon of Escherichia coli. Harris, C.L., Lui, L., Sakallah, S., DeVore, R. J. Biol. Chem. (1983) [Pubmed]
  15. Subunit structure of biodegradative threonine deaminase. Saeki, Y., Ito, S., Shizuta, Y., Hayaishi, O., Kagamiyama, H., Wada, H. J. Biol. Chem. (1977) [Pubmed]
  16. 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. Biochemistry (2000) [Pubmed]
  17. Polymorphous crystallization and diffraction of threonine deaminase from Escherichia coli. Gallagher, D.T., Eisenstein, E., Fisher, K.E., Zondlo, J., Chinchilla, D., Yu, H.D., Dill, J., Winborne, E., Ducote, K., Xiao, G., Gilliland, G.L. Acta Crystallogr. D Biol. Crystallogr. (1998) [Pubmed]
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