ArticleApplied microbiology and biotechnology2021
Engineering the Cad pathway in Escherichia coli to produce glutarate from L-lysine.
Article in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Sustainable production of glutaric acid in microbial cell factories: Current advances and future prospects.Synthetic and systems biotechnology · 2026Review
- Correlative Changes in Endogenous Polyamines and Hormones Associated with Aging in AncientPlants (Basel, Switzerland) · 2026Article
- Recombinant Escherichia coli-driven whole-cell bioconversion for selective 5-Aminopentanol production as a novel bioplastic monomer.Bioresources and bioprocessing · 2025Article
- Systems engineering of Escherichia coli for high-level glutarate production from glucose.Nature communications · 2024Article
- A Multi-Enzyme Cascade for Efficient Production of Pyrrolidone from l-Glutamate.Applied and environmental microbiology · 2023Article
- An Artificial Pathway forFrontiers in microbiology · 2022Article
- Utilization of a Wheat Sidestream for 5-Aminovalerate Production inFrontiers in bioengineering and biotechnology · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
For the efficient industrial production of glutarate, an important C5 platform chemical that is widely used in the chemical and pharmaceutical industries, a five-enzyme cascade pathway was designed and reconstructed in vitro to synthesize glutarate from L-lysine. Then, the imbalanced enzyme expression levels of L-lysine decarboxylase from Escherichia coli (EcCA), putrescine aminotransferase (KpcPA) and γ-aminovaleraldehyde dehydrogenase (KpcPD) from Klebsiella pneumoniae, and the poor catalytic efficiency of KpcPA were identified as the rate-limiting bottlenecks. To this end, ribosome binding site regulation was employed to coordinate the enzyme molar ratio of EcCA:KpcPA:KpcPD at approximately 4:8:7 (the optimum ratio obtained in vitro), and volume scanning and hydrophobicity scanning were applied to increase KpcPA activity toward cadaverine from 15.89 ± 0.52 to 75.87 ± 1.51 U·mg
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Registered trials
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