Lipohexin, a new inhibitor of prolyl endopeptidase from Moeszia lindtneri (HKI-0054) and Paecilomyces sp. (HKI-0055; HKI-0096) .2. Inhibitory activities and specificity

被引：17

作者：

Christner, C

Zerlin, M

Grafe, U

Heinze, S

Kullertz, G

Fischer, G

机构：

[1] MAX PLANCK ARBEITSGRP ENZYMOL PEPTIDBINDUNG,D-06120 HALLE,GERMANY

[2] MAX PLANCK ARBEITSGRP MOL ZELLBIOL,D-07747 JENA,GERMANY

[3] NATURSTOFF FORSCH EV,HANS KNOLL INST,D-07745 JENA,GERMANY

来源：

JOURNAL OF ANTIBIOTICS | 1997年 / 50卷 / 05期

关键词：

D O I：

10.7164/antibiotics.50.384

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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 mu M. Specificity of lipohexin (I) is indicated by the much weaker inhibitory activity against bacterial prolyl endopeptidase from Flavobacterium meningosepticum (IC50 25 mu M). No effect of lipohexin (I) was found on the activity of mechanistically related proteases such as proline specific proteases and other serine proteases.

引用

页码：384 / 389

页数：6

共 20 条

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