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通过利用意想不到的转酶反应来检测与脂质结合的酸甘油前体

Yuan Qiao¹, Matthew D Lebar, Kathrin Schirner

¹Chemical Biology Program, Harvard University , Cambridge, Massachusetts 02138, United States.

Journal of the American Chemical Society

|October 8, 2014

概括

黄金葡萄球菌PBP4作为一个转酶,将d-氨基酸纳入peptidoglycan前体. 这一发现为研究脂质结合糖素前体和抗生素机制提供了一种新的测定方法.

科学领域:

微生物学微生物学
生物化学生物化学
分子生物学分子生物学

背景情况:

青素结合蛋白 (PBPs) 对于细菌甘 (PG) 的合成和重塑至关重要.
黄金葡萄球菌拥有四个PBP,尽管与高度交叉链接的PG有遗传联系,但PBP4的确切功能仍在争论中.

研究的目的:

生物化学描述金黄色葡萄球菌PBP4.4的酶活性.
调查PBP4在将d-氨基酸纳入peptidoglycan中的作用.
开发一种用于检测低丰度脂质结合的PG前体的新型试验.

主要方法:

在实验室中使用合成脂质II的酶分析.
在体内研究评估d-氨基酸纳入细胞PG的评估.
开发和应用一种敏感测定脂结PG前体的方法.

主要成果:

在实验室中,PBP4主要作为一个转酶 (TP) 起作用.
在体内,PBP4是主要的PBP,它负责将外源的d-氨基酸纳入S. aureus PG.
PBP4表现出散乱的TP活性,在PG单体 (脂质I,脂质II) 和聚合物中交换d-氨基酸.
开发了一种新型,敏感的测试方法来检测低丰度的脂质链接PG前体.

结论:

PBP4具有转酶活性,并在d-氨基酸纳入peptidoglycan中发挥关键作用.
这项研究提供了PBP域激活酸甘单体构建块的第一个证据.
开发的试验为研究酸甘前体动态和抗生素作用机制提供了有价值的工具.

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