ArticleScience advances2024
Computation-driven redesign of an NRPS-like carboxylic acid reductase improves activity and selectivity.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- A cell-free system for 1,6-hexanediamine synthesis using bulk chemical caprolactam as the feedstock.Synthetic and systems biotechnology · 2026Article
- Biocatalytic Carboxylic Acid Reduction and Transamination in Cell-Free Lysates at High Substrate Loading.ChemSusChem · 2026Article
- From reactants to products: computational methods for biosynthetic pathway design.Synthetic and systems biotechnology · 2025Review
- Structure-guided engineering of a polyphosphate kinase 2 class III from anRSC chemical biology · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Engineering nonribosomal peptide synthetases (NRPSs) has been a "holy grail" in synthetic biology due to their modular nature and limited understanding of catalytic mechanisms. Here, we reported a computational redesign of the "gate-keeper" adenylation domain of the model NRPS-like enzyme carboxylic acid reductases (CARs) by using approximate mechanism-based geometric criteria and the Rosetta energy score. Notably,
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Registered trials
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