ArticleScientific reports2015
Engineering catechol 1, 2-dioxygenase by design for improving the performance of the cis, cis-muconic acid synthetic pathway in Escherichia coli.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 37 citations in OpenAlex.
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- Cis,cis-muconic acid production from lignin related molecules byAcinetobacter baylyi ADP1.Microbial cell factories · 2025Article
- Gut bacterium Acinetobacter sp. assists Camellia weevil with host plant adaptation by degrading tea saponin via the benzoate pathway.Microbiome · 2025Article
- EngineeringApplied and environmental microbiology · 2024Article
- Channelling carbon flux through the meta-cleavage route for improved poly(3-hydroxyalkanoate) production from benzoate and lignin-based aromatics in Pseudomonas putida H.Microbial biotechnology · 2021Article
- Crystal structures of non-oxidative decarboxylases reveal a new mechanism of action with a catalytic dyad and structural twists.Scientific reports · 2021Article
- Catechol 1,2-Dioxygenase FromFrontiers in bioengineering and biotechnology · 2021Article
- Recent Advances in Microbial Production ofBiomolecules · 2020Review
- Organic micropollutants paracetamol and ibuprofen-toxicity, biodegradation, and genetic background of their utilization by bacteria.Environmental science and pollution research international · 2018Review
- Lignin Valorization: Two Hybrid Biochemical Routes for the Conversion of Polymeric Lignin into Value-added Chemicals.Scientific reports · 2017Article
- Efficient, environmentally-friendly and specific valorization of lignin: promising role of non-radical lignolytic enzymes.World journal of microbiology & biotechnology · 2017Review
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Regulating and ameliorating enzyme expression and activity greatly affects the performance of a given synthetic pathway. In this study, a new synthetic pathway for cis, cis-muconic acid (ccMA) production was reconstructed without exogenous induction by regulating the constitutive expression of the important enzyme catechol 1,2-dioxygenase (CatA). Next, new CatAs with significantly improved activities were developed to enhance ccMA production using structure-assisted protein design. Nine mutations were designed, simulated and constructed based on the analysis of the CatA crystal structure. These results showed that mutations at Gly72, Leu73 and/or Pro76 in CatA could improve enzyme activity, and the activity of the most effective mutant was 10-fold greater than that of the wild-type CatA from Acinetobacter sp. ADP1. The most productive synthetic pathway with a mutated CatA increased the titer of ccMA by more than 25%. Molecular dynamic simulation results showed that enlarging the entrance of the substrate-binding pocket in the mutants contributed to their increased enzyme activities and thus improved the performance of the synthetic pathway.
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