Deponte Marcel
*Department of Parasitology, Ruprecht-Karls University, Im Neuenheimer Feld 324, D-69120 Heidelberg, Germany.
Biochem Soc Trans. 2014 Apr;42(2):473-8. doi: 10.1042/BST20140005.
Our current knowledge of the isomerase glyoxalase I and the thioesterase glyoxalase II is based on a variety of prokaryotic and eukaryotic (model) systems with an emphasis on human glyoxalases. During the last decade, important insights on glyoxalase catalysis and structure-function relationships have also been obtained from parasitic protists. These organisms, including kinetoplastid and apicomplexan parasites, are particularly interesting, both because of their relevance as pathogens and because of their phylogenetic diversity and host-parasite co-evolution which has led to specialized organellar and metabolic adaptations. Accordingly, the glyoxalase repertoire and properties vary significantly among parasitic protists of different major eukaryotic lineages (and even between closely related organisms). For example, several protists have an insular or non-canonical glyoxalase. Furthermore, the structures and the substrate specificities of glyoxalases display drastic variations. The aim of the present review is to highlight such differences as well as similarities between the glyoxalases of parasitic protists and to emphasize the power of comparative studies for gaining insights into fundamental principles and alternative glyoxalase functions.
我们目前对异构酶乙二醛酶I和硫酯酶乙二醛酶II的了解基于多种原核生物和真核生物（模型）系统，重点是人类乙二醛酶。在过去十年中，对乙二醛酶催化作用以及结构-功能关系的重要见解也来自寄生原生生物。这些生物，包括动质体和顶复体寄生虫，特别有趣，这既是因为它们作为病原体的相关性，也因为它们的系统发育多样性以及宿主-寄生虫共同进化导致了特殊的细胞器和代谢适应性。因此，不同主要真核生物谱系的寄生原生生物（甚至亲缘关系密切的生物体之间）的乙二醛酶种类和特性差异很大。例如，几种原生生物有一种孤立的或非典型的乙二醛酶。此外，乙二醛酶的结构和底物特异性表现出极大的差异。本综述的目的是突出寄生原生生物乙二醛酶之间的此类差异和相似之处，并强调比较研究对于深入了解基本原理和乙二醛酶替代功能的作用。
