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) | 2797-2799 |
| Number of pages | 3 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 73 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 2009 |
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Keywords
- CYP199A2
- Cytochrome p450
- Hydroxylation
- Naphthoic acid
- Oxidation
ASJC Scopus subject areas
- Biotechnology
- Biochemistry
- Molecular Biology
- Applied Microbiology and Biotechnology
- Analytical Chemistry
- Organic Chemistry
- Medicine(all)
Cite this
Biocatalytic synthesis of dihydroxynaphthoic acids by cytochrome P450 CYP199A2. / Furuya, Toshiki; Kino, Kuniki.
In: Bioscience, Biotechnology and Biochemistry, Vol. 73, No. 12, 2009, p. 2797-2799.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Biocatalytic synthesis of dihydroxynaphthoic acids by cytochrome P450 CYP199A2
AU - Furuya, Toshiki
AU - Kino, Kuniki
PY - 2009
Y1 - 2009
N2 - 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.
AB - 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.
KW - CYP199A2
KW - Cytochrome p450
KW - Hydroxylation
KW - Naphthoic acid
KW - Oxidation
UR - http://www.scopus.com/inward/record.url?scp=74349118554&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=74349118554&partnerID=8YFLogxK
U2 - 10.1271/bbb.90624
DO - 10.1271/bbb.90624
M3 - Article
VL - 73
SP - 2797
EP - 2799
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 12
ER -