ArticleJournal of industrial microbiology & biotechnology2007
Co-expression of P450 BM3 and glucose dehydrogenase by recombinant Escherichia coli and its application in an NADPH-dependent indigo production system.
Article in Journal of industrial microbiology & biotechnology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 51 citations in OpenAlex.
- Choose Your Own Adventure: A Comprehensive Database of Reactions Catalyzed by Cytochrome P450 BM3 Variants.ACS catalysis · 2024Review
- Overexpression of chaperones GroEL/ES from Escherichia coli enhances indigo biotransformation production of cytochrome P450 BM3 mutant.Biotechnology letters · 2023Article
- Enzymatic Characterization and Coenzyme Specificity Conversion of a Novel Dimeric Malate Dehydrogenase from Bacillus subtilis.The protein journal · 2023Article
- Efficient Biosynthesis of 10-Hydroxy-2-decenoic Acid Using a NAD(P)H Regeneration P450 System and Whole-Cell Catalytic Biosynthesis.ACS omega · 2022Article
- Identification of an indole biodegradation gene cluster fromFrontiers in bioengineering and biotechnology · 2022Article
- Engineering cytochrome P450 enzyme systems for biomedical and biotechnological applications.The Journal of biological chemistry · 2020Review
- Recombinant production of eukaryotic cytochrome P450s in microbial cell factories.Bioscience reports · 2018Review
- Biodegradation and Biotransformation of Indole: Advances and Perspectives.Frontiers in microbiology · 2018Review
- Versatile biocatalysis of fungal cytochrome P450 monooxygenases.Microbial cell factories · 2016Review
- NADPH-generating systems in bacteria and archaea.Frontiers in microbiology · 2015Review
- Detoxification of Indole by an Indole-Induced Flavoprotein Oxygenase from Acinetobacter baumannii.PloS one · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
P450 BM3 mutant can catalyze indole to indoxyl, and indoxyl can dimerize to form indigo. But the reaction catalyzed by P450 BM3 requires NADPH, as coenzyme regeneration is very important in this system. As we know, when glucose dehydrogenase oxidizes glucose to glucolactone, NADH or NADPH can be formed, which can contribute to NADPH regeneration in the reaction catalyzed by P450 BM3. In this paper, a recombinant Escherichia coli BL21 (pET28a (+)-P450 BM3-gdh0310) was constructed to co-express both P450 BM3 gene and glucose dehydrogenase (GDH) gene. To improve the expression level of P450 BM3 and GDH in E. coli and to avoid the complex and low-efficiency refolding operation in the purification procedure, the expression conditions were optimized. Under the optimized conditions, the maximum P450 BM3 and GDH activities amounted to 8173.13 and 0.045 U/mg protein, respectively. Then bioconversion of indole to indigo was carried out by adding indole and glucose to the culture after improved expression level was obtained under optimized conditions, and 2.9 mM (760.6 mg/L) indigo was formed with an initial indole concentration of 5 mM.
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