許多革蘭氏陽性菌的表面蛋白是經(jīng)過一種被稱為分選酶的半胱氨酸轉(zhuǎn)肽酶的作用而錨定到細(xì)胞壁上,由于表面蛋白在病原菌的致病性方面起關(guān)鍵作用,,分選酶有可能成為降低革蘭氏陽性菌致病性的藥物靶點(diǎn). 目前,通過對(duì)金黃色葡萄球菌中分選酶A (SrtA) 的研究,,已初步闡明分選酶的作用機(jī)制及其活性位點(diǎn),,與此同時(shí),一些SrtA抑制劑的初步鑒定為今后抑制劑更深層次的篩選提供了基礎(chǔ),。
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Many surface proteins of Gram-positive bacteria are anchored to the cell wall by the action of sortase enzymes, a recently discovered family of cysteine transpeptidases. As the surface proteins of pathogens are frequently required for virulence, the sortase might be a suitable target for the development of anti-Gram-positive drugs. Recently, the mechanism and active sites of sortase was elucidated by the research of sortaseA(SrtA) in Staphylococcus aureus and a series of SrtA inhibitors have been identified for providing the basis for further development of potent inhibitors.
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