{
  "id": 13009576,
  "title": "A Minimal Model of Functional Redundancy as a Route to Enzyme Specialisation",
  "url": "https://urgent.news/2026/10/08/a-minimal-model-of-functional-redundancy-as-a-route-to-enzyme",
  "topic": "science",
  "section": "Science",
  "published": "2026-10-08T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.10.02.756335v1?rss=1"
  },
  "original_language": "en",
  "account": "This research explores the concept of functional redundancy in enzymes, suggesting that proteins can become specialized while still maintaining overall organismal reaction performance. In the study's minimal model, weak enzymes initially carry out all 120 reactions, with fitness determined by the collective catalytic capacity. Mutations affect the enzymes' activity profiles, constrained by a structural incompatibility factor, without any gene duplication taking place. The researchers simulated scenarios involving five initial redundancies, two mutation kernels, and four incompatibility levels, repeating each combination across five trials and introducing 250 fixed substitutions per simulation. The findings indicate that as overall protein breadth decreases, the most effective function increases its share of activity, with mean reductions in breadth ranging from 1.59 to 3.97 under the loss-biased kernel and 6.32 to 8.16 under the symmetric kernel. This shows that specialization does not necessarily require a bias towards losing biochemical function. The model also reveals that higher redundancy helps buffer the weakest reaction performance under loss-biased mutations, while structural incompatibility has a non-monotonic effect on the specialization process. Despite the decrease in total activity, the model does not suggest that this is a conservation-based efficiency gain, highlighting that duplication is not a necessary step for specialization in this class of models.",
  "summary": "Functional overlap among enzymes could permit individual proteins to specialise while maintaining organismal reaction performance. We examine this possibility in a minimal origin--fixation model in which weak generalists jointly supply 120 reactions and fitness depends on aggregate catalytic capacity. Pleiotropic mutations act on loop-local activity profiles subject to a tunable structural…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}