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Chemical Compound Review

Thr-Val     (2R)-2-[[(2S,3R)-2-amino-3- hydroxy...

Synonyms: AC1O5312
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Disease relevance of Thr-Val

  • Kinetic analysis of enzymatic biotinylation using purified Met --> Thr/Val mutant proteins with both yeast and Escherichia coli BPLs revealed that these substitutions had a strong effect upon K(m) values but not k(cat) [1].
  • The two proteinases acted similarly, except for substrates having Thr, Val and Leu substitutions, which were better accommodated in the HIV-2 substrate binding pocket [2].

High impact information on Thr-Val

  • We replaced the invariant Gly17 residue in human neutrophil alpha-defensin 2 (HNP2) by L-Ala or one of the D-amino acids Ala, Glu, Phe, Arg, Thr, Val, or Tyr [3].
  • The serine-threonine kinase inhibitor H7 inhibited the transactivation potential of Thr-, Val-, and Asp-Stat5 to a similar extent, eliminating phosphorylation of Thr(757) as a regulatory mechanism [4].
  • We prepared a set of seven single amino acid replacement mutants of rhodopsin at position 121 (G121A, Ser, Thr, Val, Ile, Leu, and Trp) and control mutants with replacements of Gly114 or Ala117 [5].
  • Mismatches can frequently be related to large B-factors, certain types of amino acid substitutions, or the appearance of multiple minima on the side-chain potential energy surfaces and are most likely to occur for certain small residues (Ser, Thr, Val) [6].
  • In addition, binding of sec8 is dependent on its C-terminal-binding sequence namely Thr-Thr-Val (TTV) [7].

Associations of Thr-Val with other chemical compounds

  • The enantiomer of five NBD-amino acids (Ser, Thr, Val, Phe and His) could be separated by LE-CE using a 20 mM ammonium acetate buffer (pH 9.0) containing 10 mM copper acetate, 20 mM L-prolinamide and 1 mM SDS [8].

Gene context of Thr-Val

  • All members of a given Kv2, Kv3 or Kv4 potassium channel subfamily have identical amino acids at similar positions in their deep pore regions (Thr/Tyr or Thr/Val), which suggests that any difference in surface levels among members is not dictated by these amino acids [9].
  • A peptide of the composition Met, Arg, His, Gly2, Asp3, Ile, Ser3, Thr, Val was found in the digest of the wild-type amidase and was replaced in the digests of the mutant amidases by a peptide of the composition Met, Arg, His, Gly2, Asp3, Ile, Ser3, Thr, Val, Phe [10].


  1. Mutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains. Polyak, S.W., Chapman-Smith, A., Mulhern, T.D., Cronan, J.E., Wallace, J.C. J. Biol. Chem. (2001) [Pubmed]
  2. Studies on the role of the S4 substrate binding site of HIV proteinases. Tözsér, J., Gustchina, A., Weber, I.T., Blaha, I., Wondrak, E.M., Oroszlan, S. FEBS Lett. (1991) [Pubmed]
  3. Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids. Xie, C., Prahl, A., Ericksen, B., Wu, Z., Zeng, P., Li, X., Lu, W.Y., Lubkowski, J., Lu, W. J. Biol. Chem. (2005) [Pubmed]
  4. Conversion of threonine 757 to valine enhances Stat5a transactivation potential. Gowri, P.M., Ganguly, T.C., Cao, J., Devalaraja, M.N., Groner, B., Vore, M. J. Biol. Chem. (2001) [Pubmed]
  5. The effects of amino acid replacements of glycine 121 on transmembrane helix 3 of rhodopsin. Han, M., Lin, S.W., Smith, S.O., Sakmar, T.P. J. Biol. Chem. (1996) [Pubmed]
  6. Analysis of side-chain orientations in homologous proteins. Summers, N.L., Carlson, W.D., Karplus, M. J. Mol. Biol. (1987) [Pubmed]
  7. Exocyst complex subunit sec8 binds to postsynaptic density protein-95 (PSD-95): a novel interaction regulated by cypin (cytosolic PSD-95 interactor). Riefler, G.M., Balasingam, G., Lucas, K.G., Wang, S., Hsu, S.C., Firestein, B.L. Biochem. J. (2003) [Pubmed]
  8. Chiral separation of NBD-amino acids by ligand-exchange micro-channel electrophoresis. Nakajima, H., Kawata, K., Shen, H., Nakagama, T., Uchiyama, K. Analytical sciences : the international journal of the Japan Society for Analytical Chemistry. (2005) [Pubmed]
  9. Amino acids in the pore region of Kv1 potassium channels dictate cell-surface protein levels: a possible trafficking code in the Kv1 subfamily. Zhu, J., Gomez, B., Watanabe, I., Thornhill, W.B. Biochem. J. (2005) [Pubmed]
  10. Molecular basis of altered enzyme specificities in a family of mutant amidases from Pseudomonas aeruginosa. Paterson, A., Clarke, P.H. J. Gen. Microbiol. (1979) [Pubmed]
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