The transient assembly or sequestration of enzymes into clusters permits the channeling of metabolites, but requires spatiotemporal control. Liquid liquid phase separation (LLPS) has recently emerged as a fundamental concept enabling formation of such assemblies into non-membrane bound organelles. The role of LLPS in the formation of condensates containing the CO₂-fixing enzyme Rubisco has recently become appreciated. Both prokaryotic carboxysomes and eukaryotic pyrenoids enhance the carboxylation reaction by enabling the saturation of the enzyme with CO₂ gas. Biochemical reconstitution and structural biology are revealing the mechanistic basis of these photosynthetic condensates. At the same time other enzyme clusters, such as purinosomes for de-novo purine biosynthesis and G-bodies containing glycolytic enzymes, are emerging to behave like phase-separated systems. In the near future we anticipate details of many more such metabolic condensates to be revealed, deeply informing our ability to influence metabolic fluxes.

酶的瞬时组装或螯合成簇允许代谢产物的通道化，但需要时空控制。液相-液相分离（LLPS）最近已成为一个基本概念，能够将此类组件形成非膜结合的细胞器。LLPS在含有CO ₂固定酶Rubisco的缩合物的形成中的作用最近已被人们所认识。通过使酶被CO ₂饱和，原核羧基体和真核类胡萝卜素均可增强羧化反应加油站。生化重建和结构生物学正在揭示这些光合冷凝物的机理基础。同时，其他酶簇，例如用于新的嘌呤生物合成的嘌呤体和含有糖酵解酶的G体，也开始表现出相分离系统的作用。在不久的将来，我们预计将揭示更多此类代谢冷凝物的细节，从而深刻告知我们影响代谢通量的能力。