Effects of Ym-51084 and Ym-51085, New Inhibitors Produced byStreptomyces Sp. Q21705, on Cathepsin L
| Autor: | Kenichi Yasumuro, Kyoko Teramura, Kenji Abe, Masaya Orita, Hisao Matsumoto |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Magnetic Resonance Spectroscopy
Cathepsin L medicine.medical_treatment Cysteine Proteinase Inhibitors Spectrometry Mass Fast Atom Bombardment Kidney Biochemistry Streptomyces Cathepsin A Cathepsin B Cathepsin C Cathepsin O Endopeptidases Papain Ic50 values medicine Humans Carbon Isotopes Protease Molecular Structure biology Chemistry biology.organism_classification Cathepsins Protease inhibitor (biology) Enzyme Activation Cysteine Endopeptidases biology.protein Molecular Medicine Oligopeptides Hydrogen medicine.drug |
| Zdroj: | Journal of Enzyme Inhibition. 11:115-121 |
| ISSN: | 8755-5093 |
| DOI: | 10.3109/14756369609036538 |
| Popis: | The structures of YM-51084 and YM-51085, new protease inhibitors produced by Streptomyces sp. Q21705, were determined by 1H- and 13C-NMR and mass spectrometry. Both were characterized by the basic structures of an acyl-tripeptide. YM-51084 was elucidated to be isovaleryl-tyrosyl-valyl-phenylalaninal and YM-51085 was the reduced phenylalaninol form of YM-51084. These compounds proved to strongly inhibit human kidney cathepsin L; the IC50 values being 9.6 x 10(-9) M and 3.5 x 10(-7) M, respectively. |
| Databáze: | OpenAIRE |
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