A metabolon that GATEs

IF 48.3 1区化学 Q1 CHEMISTRY, PHYSICAL

Nature Catalysis Pub Date : 2026-06-25 DOI:10.1038/s41929-026-01553-4

Alisdair R. Fernie, Guillaume Decros

引用次数: 0

Abstract

The chalcone synthase (CHS)–chalcone isomerase-like protein (CHIL) complex is well defined, however, regulatory mechanisms remain obscure for this complex, as for most metabolons. Now, evaluating transient dynamics of this metabolon reveals that CHS undergoes rapid reversible binding cycles with CHIL and that this transiently displaces the coenzyme A inhibitor from the binding tunnel through competitive occupation, reshapes the CHS active site and guides the intermediate to product reaction thereby regulating catalysis in real time.

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这是一个新陈代谢的过程

查尔酮合成酶(CHS) -查尔酮异构酶样蛋白（CHIL）复合体是明确的，然而，与大多数代谢物一样，该复合体的调控机制仍然不清楚。现在，对这种代谢的瞬态动力学的评估表明，CHS与CHIL经历了快速的可逆结合周期，通过竞争性占领，CHS在结合通道中短暂地取代了辅酶A抑制剂，重塑了CHS的活性位点，引导中间体进入产物反应，从而实时调节催化作用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Nature Catalysis Chemical Engineering-Bioengineering

CiteScore

52.10

自引率

1.10%

发文量

140

期刊介绍： Nature Catalysis serves as a platform for researchers across chemistry and related fields, focusing on homogeneous catalysis, heterogeneous catalysis, and biocatalysts, encompassing both fundamental and applied studies. With a particular emphasis on advancing sustainable industries and processes, the journal provides comprehensive coverage of catalysis research, appealing to scientists, engineers, and researchers in academia and industry. Maintaining the high standards of the Nature brand, Nature Catalysis boasts a dedicated team of professional editors, rigorous peer-review processes, and swift publication times, ensuring editorial independence and quality. The journal publishes work spanning heterogeneous catalysis, homogeneous catalysis, and biocatalysis, covering areas such as catalytic synthesis, mechanisms, characterization, computational studies, nanoparticle catalysis, electrocatalysis, photocatalysis, environmental catalysis, asymmetric catalysis, and various forms of organocatalysis.