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Chemical Compound Review

trapoxin     (3S,6S,9S,12R)-3,6-dibenzyl- 9-[6-[(2S)...

Synonyms: Trapoxin B, AG-K-55544, CHEMBL2000089, NSC-700657, CTK4B8393, ...
 
 
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High impact information on NSC700657

  • HDAC6, which is insensitive to trapoxin B, specifically interacted with the carboxy terminus of Runx2 [1].
  • This tandem organization of two catalytic domains confers resistance to the inhibitors trapoxin B and sodium butyrate, which potently inhibit the deacetylase activity of all other HDAC members [2].
  • The structures were found to be new cyclotetrapeptides, cyclo[(S)-phenylalanyl-(S)-phenylalanyl-(R)-pipecolinyl- (2S,9S)-2-amino-8-oxo-9,10-epoxydecanoyl-] for trapoxin A and cyclo[(S)-phenylalanyl-(S)-phenylalanyl-(R)-prolyl-2- amino-8-oxo-9,10-epoxydecanoyl-] for trapoxin B, by X-ray analysis, mass spectrometric, NMR and chemical studies [3].

References

  1. Runx2 (Cbfa1, AML-3) interacts with histone deacetylase 6 and represses the p21(CIP1/WAF1) promoter. Westendorf, J.J., Zaidi, S.K., Cascino, J.E., Kahler, R., van Wijnen, A.J., Lian, J.B., Yoshida, M., Stein, G.S., Li, X. Mol. Cell. Biol. (2002) [Pubmed]
  2. Molecular cloning and characterization of a novel histone deacetylase HDAC10. Guardiola, A.R., Yao, T.P. J. Biol. Chem. (2002) [Pubmed]
  3. Isolation and structural elucidation of new cyclotetrapeptides, trapoxins A and B, having detransformation activities as antitumor agents. Itazaki, H., Nagashima, K., Sugita, K., Yoshida, H., Kawamura, Y., Yasuda, Y., Matsumoto, K., Ishii, K., Uotani, N., Nakai, H. J. Antibiot. (1990) [Pubmed]
 
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