ArticleAntonie van Leeuwenhoek2013
High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production.
Article in Antonie van Leeuwenhoek, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 67 citations in OpenAlex.
- Study on the degradation pathway of benzo[a]pyrene byFrontiers in microbiology · 2025Article
- Investigating the quaternary structure of a homomultimeric catechol 1,2-dioxygenase: An integrative structural biology study.PloS one · 2025Article
- EngineeringApplied and environmental microbiology · 2024Article
- Biodegradation of isoproturon by Escherichia coli expressing a Pseudomonas putida catechol 1,2-dioxygenase gene.AMB Express · 2023Article
- Characterization of Catechol-1,2-Dioxygenase (Acdo1p) FromFrontiers in microbiology · 2022Article
- Biological Inspirations: Iron Complexes Mimicking the Catechol Dioxygenases.Materials (Basel, Switzerland) · 2021Review
- Catechol 1,2-Dioxygenase FromFrontiers in bioengineering and biotechnology · 2021Article
- Statistical Optimisation of Phenol Degradation and Pathway Identification through Whole Genome Sequencing of the Cold-Adapted Antarctic Bacterium,International journal of molecular sciences · 2020Article
- Comparative Genomics ofInternational journal of molecular sciences · 2020Article
- Degradation Mechanism of 2,4-Dichlorophenol by Fungi Isolated from Marine Invertebrates.International journal of molecular sciences · 2020Article
- Structural and functional characterization of an intradiol ring-cleavage dioxygenase from the polyphagous spider mite herbivore Tetranychus urticae Koch.Insect biochemistry and molecular biology · 2019Article
- Catechol 1,2-Dioxygenase is an Analogue of Homogentisate 1,2-Dioxygenase inInternational journal of molecular sciences · 2018Article
- Organic micropollutants paracetamol and ibuprofen-toxicity, biodegradation, and genetic background of their utilization by bacteria.Environmental science and pollution research international · 2018Review
- Metabolic engineering of Corynebacterium glutamicum for the production of cis, cis-muconic acid from lignin.Microbial cell factories · 2018Article
- Biotransformation of benzo[a]pyrene by the thermophilic bacterium Bacillus licheniformis M2-7.World journal of microbiology & biotechnology · 2018Article
- Biodegradation of alkaline lignin byBiotechnology for biofuels · 2017Article
- Genome sequencing reveals mechanisms for heavy metal resistance and polycyclic aromatic hydrocarbon degradation in Delftia lacustris strain LZ-C.Ecotoxicology (London, England) · 2016Article
- Purification and Characterization of Catechol 1,2-Dioxygenase from Acinetobacter sp. Y64 Strain and Escherichia coli Transformants.The protein journal · 2015Article
- Engineering catechol 1, 2-dioxygenase by design for improving the performance of the cis, cis-muconic acid synthetic pathway in Escherichia coli.Scientific reports · 2015Article
- Immobilization as a strategy for improving enzyme properties-application to oxidoreductases.Molecules (Basel, Switzerland) · 2014Review
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
This is the first report of a catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 with high activity against catechol and its methyl derivatives. This enzyme was maximally active at pH 8.0 and 40 °C and the half-life of the enzyme at this temperature was 3 h. Kinetic studies showed that the value of K m and V max was 12.8 μM and 1,218.8 U/mg of protein, respectively. During our studies on kinetic properties of the catechol 1,2-dioxygenase we observed substrate inhibition at >80 μM. The nucleotide sequence of the gene encoding the S. maltophilia strain KB2 catechol 1,2-dioxygenase has high identity with other catA genes from members of the genus Pseudomonas. The deduced 314-residue sequence of the enzyme corresponds to a protein of molecular mass 34.5 kDa. This enzyme was inhibited by competitive inhibitors (phenol derivatives) only by ca. 30 %. High tolerance against condition changes is desirable in industrial processes. Our data suggest that this enzyme could be of use as a tool in production of cis,cis-muconic acid and its derivatives.
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