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首页> 外文期刊>Journal of bacteriology >Biochemical properties of a novel metalloprotease from Staphylococcus hyicus subsp. hyicus involved in extracellular lipase processing.
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Biochemical properties of a novel metalloprotease from Staphylococcus hyicus subsp. hyicus involved in extracellular lipase processing.

机译：新型葡萄球菌hypsus亚种的金属蛋白酶的生化特性。 hyicus参与细胞外脂肪酶的加工。

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Two extracellular proteases from Staphylococcus hyicus subsp. hyicus, ShpI and ShpII, have been characterized. ShpI is a neutral metalloprotease with broad substrate specificity; the gene has been cloned and sequenced. ShpII, characterized here, is mainly produced in the late logarithmic growth phase in contrast to ShpI, which is mainly produced in the late stationary growth phase. ShpII was purified from culture medium of S. hyicus by ammonium sulfate precipitation and DEAE-Sepharose chromatography. The molecular mass, estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was 34 kDa. The temperature optimum of ShpII was 55 degrees C, and the pH optimum was 7.4. ShpII, a neutral metalloprotease, was strongly inhibited by zinc and calcium chelators. The amino-terminal sequence of the active enzyme was similar to the corresponding region of a Staphylococcus epidermidis metalloprotease. The substrate specificity of ShpII was similar to that of thermolysin-like proteases, with the exception that ShpII also recognized aromatic amino acids. We demonstrated in vitro that ShpII, but not ShpI, cleaved the 86-kDa S. hyicus subsp. hyicus prolipase between Thr-245 and Val-246 to generate the mature 46-kDa lipase. Results of additional in vivo experiments supported the model that ShpII is necessary for the extracellular processing and maturation of S. hyicus subsp. hyicus lipase.
机译：来自葡萄球菌亚种的两种胞外蛋白酶。 hyicus，ShpI和ShpII，已被表征。 ShpI是一种中性金属蛋白酶，具有广泛的底物特异性。该基因已被克隆并测序。与此处主要在静止生长后期产生的ShpI相反，此处表征的ShpII主要在对数生长期的后期产生。通过硫酸铵沉淀和DEAE-Sepharose色谱法从葡萄球菌的培养基中纯化ShpII。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计的分子量为34kDa。 ShpII的最适温度为55℃，最适pH为7.4。 ShpII，一种中性金属蛋白酶，被锌和钙螯合剂强烈抑制。活性酶的氨基末端序列类似于表皮葡萄球菌金属蛋白酶的相应区域。 ShpII的底物特异性与类似嗜热菌蛋白酶的底物特异性相似，只是ShpII也可以识别芳香族氨基酸。我们在体外证明，ShpII而不是ShpI切割了86 kDa的hy.us hyusus亚种。 Thr-245和Val-246之间的hyicus脂肪酶产生成熟的46-kDa脂肪酶。其他体内实验的结果支持了模型，即ShpII对于hy.us菌亚种的细胞外加工和成熟是必需的。 hyicus脂肪酶。

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