Lipohexin, a new inhibitor of prolyl endopeptidase from Moeszia lindtneri (HKI-0054) and Paecilomyces sp. (HKI-0055; HKI-0096). II. Inhibitory activities and specificity
The new proline-containing lipohexapeptide lipohexin (I) isolated from three fungal strains, Moeszia lindtneri (HKI-0054) and Paecilomyces sp. (HKI-0055 and HKI-0096) is a competitive inhibitor of prolyl endopeptidase (PEP) from human placenta with IC50 of 3.5 microM. Specificity of lipohexin (I) is...
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| Veröffentlicht in: | Journal of antibiotics 1997-05, Vol.50 (5), p.384-389 |
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| container_issue | 5 |
| container_start_page | 384 |
| container_title | Journal of antibiotics |
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| creator | CHRISTNER, C ZERLIN, M GRÄFE, U HEINZE, S KÜLLERT, G FISCHER, G |
| description | The new proline-containing lipohexapeptide lipohexin (I) isolated from three fungal strains, Moeszia lindtneri (HKI-0054) and Paecilomyces sp. (HKI-0055 and HKI-0096) is a competitive inhibitor of prolyl endopeptidase (PEP) from human placenta with IC50 of 3.5 microM. Specificity of lipohexin (I) is indicated by the much weaker inhibitory activity against bacterial prolyl endopeptidase from Flavobacterium meningosepticum (IC50 25 microM). No effect of lipohexin (I) was found on the activity of mechanistically related proteases such as proline specific proteases and other serine proteases. |
| doi_str_mv | 10.7164/antibiotics.50.384 |
| format | Article |
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(HKI-0055; HKI-0096). II. Inhibitory activities and specificity</atitle><jtitle>Journal of antibiotics</jtitle><addtitle>J Antibiot (Tokyo)</addtitle><date>1997-05</date><risdate>1997</risdate><volume>50</volume><issue>5</issue><spage>384</spage><epage>389</epage><pages>384-389</pages><issn>0021-8820</issn><eissn>1881-1469</eissn><coden>JANTAJ</coden><abstract>The new proline-containing lipohexapeptide lipohexin (I) isolated from three fungal strains, Moeszia lindtneri (HKI-0054) and Paecilomyces sp. (HKI-0055 and HKI-0096) is a competitive inhibitor of prolyl endopeptidase (PEP) from human placenta with IC50 of 3.5 microM. Specificity of lipohexin (I) is indicated by the much weaker inhibitory activity against bacterial prolyl endopeptidase from Flavobacterium meningosepticum (IC50 25 microM). 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| subjects | Animals Anti-Bacterial Agents - pharmacology Antibacterial agents Antibiotics (antibacterial agents, antifungal agents) Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents Antibiotics. Antiinfectious agents. Antiparasitic agents Applied microbiology Biological and medical sciences Cattle Flavobacterium - enzymology Fundamental and applied biological sciences. Psychology Humans Lipoproteins - pharmacology Medical sciences Microbiology Mitosporic Fungi Paecilomyces Peptides Pharmacology. Drug treatments Serine Endopeptidases - metabolism Substrate Specificity Swine |
| title | Lipohexin, a new inhibitor of prolyl endopeptidase from Moeszia lindtneri (HKI-0054) and Paecilomyces sp. (HKI-0055; HKI-0096). II. Inhibitory activities and specificity |
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