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磷酯酶D结构与其活性的关系 被引量:2

The Structure of PLD And Its Relationship with the Enzyme Activity
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摘要 磷酯酶D(PLD)作为一种磷酯酶,不仅能催化甘油磷酯末端的磷酸二酯键水解,而且在合适醇类受体存在的情况下,PLD还可以催化转磷酯酰基反应,将磷酯酰基转移到醇类上,生成相应的磷酯衍生物。但不同来源的PLD其转酰基活性的潜能不同,这主要与PLD的HKD模序及环形区域结构相关。本文就PLD的结构与其活性的关系予以简要综述。 As a phospholipase,phospholipase D(PLD) catalyzes the hydrolysis of glyeerophospho-lipids at the terminal phesphodiester bond resulting in the production ofphosphatidic acid and free choline. In the presence of a suitable acceptor alcohol,most PLDs are able to transfer the phosphatidyl moiety to this alcohol in a so-called transphosphatidylation reaction. The transesteritication propensity of PLD in different types and sources is different. This difference mainly depend on the spatial surrounding of HKD motifys and the annular region. This review summarizes the structure of PLD and the relationship between the structure and enzyme activity.
作者 左娟 朱玲
出处 《医学综述》 2009年第12期1766-1768,共3页 Medical Recapitulate
基金 福建省科技攻关重点项目(2004Y010) 福建省产业技术研究开发项目(200504)
关键词 磷酯酶D 转磷酯酰基反应 HKD模序 Phospholipase D Transphosphatidylation activity HKD motif
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参考文献21

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同被引文献18

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