马链球菌兽疫亚种的细胞质膜脂蛋白LppC具有酸性磷酸酶的功能。
Cytoplasmic membrane lipoprotein LppC of Streptococcus equisimilis functions as an acid phosphatase.
作者信息
Malke H
机构信息
Institute for Molecular Biology, Jena University, Germany.
出版信息
Appl Environ Microbiol. 1998 Jul;64(7):2439-42. doi: 10.1128/AEM.64.7.2439-2442.1998.
Abstract
The function of the streptococcal cytoplasmic membrane lipoprotein, LppC, was identified with isogenic Streptococcus equisimilis H46A and Escherichia coli JM109 strain pairs differing in whether they contained [H46A and JM109(pLPP2)] or lacked (H46A lppC::pLPP10 and JM109) the functional lppC gene for comparative phosphatase determinations under acidic conditions. lppC-directed acid phosphatase activity was demonstrated zymographically and by specific enzymatic activity assays, with whole cells or cell membrane preparations as enzyme sources. LppC acid phosphatase showed optimum activity at pH 5, and the enzyme activity was unaffected by Triton X-100, L-(+)-tartaric acid, or EDTA. Database searches revealed significant structural homology of LppC to the Streptococcus pyogenes LppA, Flavobacterium meningosepticum OplA, Helicobacter pylori HP1285, and Haemophilus influenzae Hel [e (P4)] proteins. These results suggest a possible function for these proteins and establish a novel function of streptococcal cell membrane lipoproteins.
摘要
利用等基因的马链球菌兽疫亚种H46A和大肠杆菌JM109菌株对来鉴定链球菌细胞质膜脂蛋白LppC的功能。这两种菌株对的区别在于，它们是否含有[H46A和JM109(pLPP2)]或缺乏（H46A lppC::pLPP10和JM109）功能性lppC基因，以便在酸性条件下进行比较磷酸酶测定。通过酶谱分析以及使用全细胞或细胞膜制剂作为酶源的特异性酶活性测定，证实了lppC导向的酸性磷酸酶活性。LppC酸性磷酸酶在pH 5时显示出最佳活性，并且该酶活性不受Triton X-100、L-(+)-酒石酸或EDTA的影响。数据库搜索显示，LppC与化脓性链球菌LppA、脑膜炎败血黄杆菌OplA、幽门螺杆菌HP1285和流感嗜血杆菌Hel [e (P4)]蛋白具有显著的结构同源性。这些结果提示了这些蛋白质的一种可能功能，并确立了链球菌细胞膜脂蛋白的一种新功能。
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