Abstract
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.
Original language | English (US) |
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Pages (from-to) | 89-106 |
Number of pages | 18 |
Journal | Annual review of biochemistry |
Volume | 91 |
DOIs | |
State | Published - 2022 |
All Science Journal Classification (ASJC) codes
- Biochemistry