Uesugi Yoshiko, Hatanaka Tadashi
Research Institute for Biological Sciences (RIBS), Kaga-gun, Okayama, Japan.
Biochim Biophys Acta. 2009 Sep;1791(9):962-9. doi: 10.1016/j.bbalip.2009.01.020. Epub 2009 Feb 4.
Phospholipase D (PLD) plays various roles in important biological processes and physiological functions, including cell signaling. Streptomyces PLDs show significant sequence similarity and belong to the PLD superfamily containing two catalytic HKD motifs. These PLDs have conserved catalytic regions and are among the smallest PLD enzymes. Therefore, Streptomyces PLDs are thought to be suitable models for studying the reaction mechanism among PLDs from other sources. Furthermore, Streptomyces PLDs present advantages related to their broad substrate specificity and ease of enzyme preparation. Moreover, the tertiary structure of PLD has been elucidated only for PLD from Streptomyces sp. PMF. This article presents a review of recently reported studies of the mechanism of the catalytic reaction, substrate recognition, substrate specificity and stability of Streptomyces PLD using various protein engineering methods and surface plasmon resonance analysis.
磷脂酶D（PLD）在包括细胞信号传导在内的重要生物学过程和生理功能中发挥着多种作用。链霉菌PLD表现出显著的序列相似性，属于包含两个催化HKD基序的PLD超家族。这些PLD具有保守的催化区域，是最小的PLD酶之一。因此，链霉菌PLD被认为是研究其他来源PLD反应机制的合适模型。此外，链霉菌PLD具有底物特异性广泛和酶制备容易等优点。而且，仅对来自链霉菌属PMF的PLD阐明了其三级结构。本文综述了最近报道的利用各种蛋白质工程方法和表面等离子体共振分析对链霉菌PLD催化反应机制、底物识别、底物特异性和稳定性的研究。
