Abstract
CYP199A2, a bacterial P450 monooxygenase from Rhodopseudomonas palustris, was found to exhibit oxidation activity towards three hydroxynaphthoic acids. Whole cells of the recombinant Escherichia coli strain expressing CYP199A2 efficiently catalyzed the regioselective oxidation of 1-, 3-, and 6-hydroxy-2-naphthoic acids to produce 1,7-, 3,7-, and 6,7-dihydroxynaphthoic acid respectively. These results suggest that CYP199A2 might be a useful oxidation biocatalyst for the synthesis of dihydroxynaphthoic acids.
| Original language | English |
|---|---|
| Pages (from-to) | 2796-2799 |
| Number of pages | 4 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 73 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 2009 |
Keywords
- CYP199A2
- Cytochrome p450
- Hydroxylation
- Naphthoic acid
- Oxidation
ASJC Scopus subject areas
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry