| Autor: |
Cheong TK; Department of Microbiology, Michigan State University, East Lansing 48824-1101, USA., Oriel PJ |
| Jazyk: |
angličtina |
| Zdroj: |
Applied biochemistry and biotechnology [Appl Biochem Biotechnol] 2000 Spring; Vol. 84-86, pp. 903-15. |
| DOI: |
10.1385/abab:84-86:1-9:903 |
| Abstrakt: |
A 3.6-kb fragment of Bacillus stearothermophilus BR388 chromosomal DNA that confers growth on limonene to Escherichia coli has been sequenced, revealing a single open reading frame encoding a single subunit limonene hydroxylase containing 444 amino acid residues. This enzyme proved capable of limonene hydroxylation to a mixture of carveol and perillyl alcohol as well as dehydrogenation of these products to carvone and perillyl aldehyde. Oxygen, FAD, and NADH were found to stimulate the hydroxylation reaction in cell extracts, and NAD+ stimulated the dehydrogenase reaction. In two-phase bioconversions using viable E. coli cells over-expressing the limonene hydroxylase, perillyl alcohol and carvone were the principal products observed. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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