Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, USA; email:
Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, Pennsylvania, USA.
Annu Rev Biochem. 2022 Jun 21;91:89-106. doi: 10.1146/annurev-biochem-032620-105728. Epub 2022 Mar 23.
Over the past fifteen years, we have unveiled a new mechanism by which cells achieve greater efficiency in de novo purine biosynthesis. This mechanism relies on the compartmentalization of de novo purine biosynthetic enzymes into a dynamic complex called the purinosome. In this review, we highlight our current understanding of the purinosome with emphasis on its biophysical properties and function and on the cellular mechanisms that regulate its assembly. We propose a model for functional purinosomes in which they consist of at least ten enzymes that localize near mitochondria and carry out de novo purine biosynthesis by metabolic channeling. We conclude by discussing challenges and opportunities associated with studying the purinosome and analogous metabolons.
在过去的十五年中,我们揭示了细胞在从头合成嘌呤过程中提高效率的新机制。这个机制依赖于将从头合成嘌呤的酶分隔到一个称为嘌呤体的动态复合物中。在这篇综述中,我们重点介绍了嘌呤体的生物物理特性和功能,以及调节其组装的细胞机制,强调了我们对嘌呤体的现有理解。我们提出了一个功能性嘌呤体的模型,其中至少有十种酶定位于线粒体附近,并通过代谢沟道进行从头合成嘌呤。最后,我们讨论了研究嘌呤体和类似代谢物的挑战和机遇。