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Chemical Compound Review

Probestin     (2S)-1-[(2S)-1-[(2S)-2- [[(2S,3R)-3-amino-2...

Synonyms: CHEMBL1941150, SureCN12609366, AC1L2WMB, LS-118890, 123652-87-9
 
 
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Disease relevance of Probestin

  • Probestin, a new inhibitor of aminopeptidase M, has been isolated from the culture broth of Streptomyces azureus MH663-2F6 [1].
 

High impact information on Probestin

  • We show that specific inhibitors of APN, probestin and actinonin, strongly decrease DNA synthesis in phytohaemagglutinin (PHA)-stimulated T-cells [2].
  • Zn2+ ions, sulfhydryl reagents, and aminopeptidase inhibitors, especially probestin, inhibited the rat DPP III more potently [3].
  • Probestin, a new inhibitor of aminopeptidase M, produced by Streptomyces azureus MH663-2F6. I. Taxonomy, production, isolation, physico-chemical properties and biological activities [4].
  • The fragmentation pattern shown in the mass spectrum and the chemical analysis on probestin clarified the amino acid sequence [1].
  • Inhibition studies of our laboratory, using bestatin, actinonin and probestin, also demonstrated an essential role of AP-N in regulation of T cell growth [5].
 

Biological context of Probestin

  • 1) 50% of total Ala-pNA hydrolysis of viable cells was found to be due to the ectoenzyme APN as revealed by titration with the new inhibitor probestin in comparison to purified APN from human kidney (Ki value 6.5 nM) [6].

References

  1. Probestin, a new inhibitor of aminopeptidase M, produced by Streptomyces azureus MH663-2F6. II. Structure determination of probestin. Yoshida, S., Nakamura, Y., Naganawa, H., Aoyagi, T., Takeuchi, T. J. Antibiot. (1990) [Pubmed]
  2. Induction of the membrane alanyl aminopeptidase gene and surface expression in human T-cells by mitogenic activation. Lendeckel, U., Wex, T., Reinhold, D., Kähne, T., Frank, K., Faust, J., Neubert, K., Ansorge, S. Biochem. J. (1996) [Pubmed]
  3. Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences. Abramić, M., Schleuder, D., Dolovcak, L., Schröder, W., Strupat, K., Sagi, D., Peter-Katalini, J., Vitale, L. Biol. Chem. (2000) [Pubmed]
  4. Probestin, a new inhibitor of aminopeptidase M, produced by Streptomyces azureus MH663-2F6. I. Taxonomy, production, isolation, physico-chemical properties and biological activities. Aoyagi, T., Yoshida, S., Nakamura, Y., Shigihara, Y., Hamada, M., Takeuchi, T. J. Antibiot. (1990) [Pubmed]
  5. Membrane-bound peptidases of lymphocytes: functional implications. Ansorge, S., Schön, E., Kunz, D. Biomed. Biochim. Acta (1991) [Pubmed]
  6. Aminopeptidase N (CD13, EC 3.3.4.11.2) occurs on the surface of resting and concanavalin A-stimulated lymphocytes. Kunz, D., Bühling, F., Hütter, H.J., Aoyagi, T., Ansorge, S. Biol. Chem. Hoppe-Seyler (1993) [Pubmed]
 
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