Evidence map›Paper›PMID 42281556›Full record

ArticlePRX life2025

Sticky enzymes: increased metabolic efficiency via substrate-dependent enzyme clustering.

Alejandro Martínez-Calvo, Jello Zhou, Yaojun Zhang, Ned S Wingreen

Abstract read
In one paragraph

Article in PRX life, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Accelerated Ostwald Ripening by Chemical Activity.Journal of the American Chemical Society · 2025
    Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Alejandro Martínez-CalvoPrinceton Center for Theoretical Science, Princeton University, Princeton, NJ 08544, USA.ORCID 0000-0002-2109-8145
Jello ZhouDepartment of Physics, Princeton University, Princeton, NJ 08544, USA.ORCID 0009-0005-6416-6565
Yaojun ZhangDepartment of Physics and Astronomy, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0003-4587-6834
Ned S WingreenPrinceton Center for Theoretical Science, Princeton University, Princeton, NJ 08544, USA.ORCID 0000-0001-7384-2821

Funding

Learning principles from the pyrenoid, a phase-separated organelleR01GM140032 · NIGMS · PRINCETON UNIVERSITY · PI JONIKAS, MARTIN CASIMIR, WINGREEN, NED S · 2021 to 2024
$2.0M
NIGMS NIH HHS R01 GM140032
6 · The paper itself

Abstract

Coclustering of subsequent enzymes in a pathway can accelerate the processing of metabolic intermediates, with benefits including increased pathway fluxes, reduced toxicity, and sensitive branch-point regulation. While the optimal organization of such clusters has been explored theoretically, little is known about how to achieve such organization inside cells. Here we propose that phase-separating enzymes can self-organize into nearly-optimally sized and spaced clusters, provided that their "stickiness" is regulated by local substrate availability. In a nutshell, enzyme clusters only form when and where they are needed to process substrate. We study a mathematical model that implements this scheme for simple metabolic pathways, including all thermodynamic constraints. We find that pathway fluxes can be increased by 50 to 1000-fold and toxic metabolites can be decreased by 10 to 100-fold, at realistic enzyme densities. Finally, we discuss how enzyme "stickiness" could be allosterically regulated. This study presents a self-organization strategy that goes beyond current paradigms for natural and engineered enzyme clusters, and thus represents a motivating challenge to the fields of synthetic biology and metabolic engineering.

Identifiers

PMID42281556
PMCPMC13251717

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.