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Serralysin inhibitors have been proposed as potent drugs against many diseases and may help to prevent further development of antibiotic-resistant pathogenic bacteria. In this study, a novel serralysin inhibitor gene, l up I, was cloned from the marine bacterium F lavobacterium sp. YS-80-122 and expressed in Escherichia coli. The deduced serralysin inhibitor, Lup I, shows 40% amino acid identity to other reported serralysin inhibitors. Multiple sequence alignment and phylogenetic analysis of Lup I with other serralysin inhibitors indicated that Lup I was a novel type of serralysin inhibitor. The inhibitory constant for Lup I towards its target metalloprotease was 0.64 μmol/L. Lup I was thermostable at high temperature, in which 35.6%–90.7% of its inhibitory activity was recovered after treatment at 100°C for 1–60 min followed by incubation at 0°C. This novel inhibitor may represent a candidate drug for the treatment of serralysin-related infections. 相似文献
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