|Hilker, B - UNIV OF KY, LEXINGTON|
|Fukushige, H - UNIV OF KY, LEXINGTON|
|Hildebrand, D - UNIV OF KY, LEXINGTON|
Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: May 16, 2007
Publication Date: May 16, 2007
Citation: Hilker, B.L., Fukushige, H., Hou, C.T., Hildebrand, D.L. 2007. Some properties of a self-sufficient cytochrome P-450 monooxygenase from Bacillus megaterium NRRL B-21660, strain ALA2 [abstract]. American Oil Chemists' Society. Bio-1, #6. Technical Abstract: Bacillus megaterium NRRL B-21660, strain ALA2, produces many new oxygenated unsaturated fatty acids from linoleic acid with potential applications such as specialty chemicals and biomedicals. In order to utilize the enzymes involved in this pathway for the production of these new fatty acid products on a large scale, metabolic engineering is being pursued. A variant of the well characterized BM3 cytochrome P-450 monooxygenase was cloned from B. megaterium ALA2. The ALA2 BM3 gene is 3150 nucleotides and encodes a polypeptide of 1049 amino acids. It is 94.0% identical to the wild type BM3 gene on a nucleotide basis and 97.1% identical on an amino acid sequence basis. The ALA2 BM3 gene has been expressed in E. coli and the expression products are being analyzed.