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Gene Review

OMR1  -  threonine dehydratase

Arabidopsis thaliana

Synonyms: L-O-methylthreonine resistant 1, THREONINE DEHYDRATASE/DEAMINASE
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High impact information on OMR1

  • Rescue of tha2 mutants and tha1 tha2 double mutants by overproduction of feedback-insensitive Thr deaminase (OMR1) shows that Gly formation by THA1 and THA2 is not essential in Arabidopsis [1].
  • Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool [1].
  • Nondenaturant gel filtration, polyacrylamide gel electrophoresis, and mass spectrometry experiments demonstrated that binding of isoleucine on TD induces dimerization of the enzyme, whereas tetramerization is restored by addition of a high valine concentration [2].
  • While all of the four omr1 alleles conferred resistance to elevated concentrations of OMT, the progeny of omr1-1 initial transformants exhibited a bushy phenotype at the rosette stage [3].
  • The mutant TD forms consisted of our previously isolated double mutant, omr1-1 , and three new site-directed mutants, omr1-5 , omr1-7 , and omr1-8 with single point mutations [3].

Associations of OMR1 with chemical compounds


  1. Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool. Joshi, V., Laubengayer, K.M., Schauer, N., Fernie, A.R., Jander, G. Plant Cell (2006) [Pubmed]
  2. Biochemical and mass spectrometric evidence for quaternary structure modifications of plant threonine deaminase induced by isoleucine. Halgand, F., Wessel, P.M., Laprévote, O., Dumas, R. Biochemistry (2002) [Pubmed]
  3. 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., Mourad, G.S. Plant Mol. Biol. (2004) [Pubmed]
  4. PHA production, from bacteria to plants. Valentin, H.E., Broyles, D.L., Casagrande, L.A., Colburn, S.M., Creely, W.L., DeLaquil, P.A., Felton, H.M., Gonzalez, K.A., Houmiel, K.L., Lutke, K., Mahadeo, D.A., Mitsky, T.A., Padgette, S.R., Reiser, S.E., Slater, S., Stark, D.M., Stock, R.T., Stone, D.A., Taylor, N.B., Thorne, G.M., Tran, M., Gruys, K.J. Int. J. Biol. Macromol. (1999) [Pubmed]
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