Cloning, expression in yeast, and functional characterization of CYP76A4, a novel cytochrome P450 of petunia that catalyzes (omega-1)-hydroxylation of lauric acid.
A cDNA clone of a novel cytochrome P450, CYP76A4, was isolated from Petunia hybrida. The cDNA clone contained an open reading frame (ORF) encoding a predicted 510 amino acid polypeptide. The CYP76A4 cDNA was expressed in yeast Saccharomyces cerevisiae AH22. Recombinant yeast microsomes containing the CYP76A4 hemoprotein were found to catalyze (omega-1)-hydroxylation of lauric acid.
Tamaki
Katsutomo
K
Laboratory of Biotechnology, Hyogo Prefectural Research Institute for Agriculture, Kasai-shi, Hyogo, Japan.
Imaishi
Hiromasa
H
Ohkawa
Hideo
H
Oono
Kiyoharu
K
Sugimoto
Mikihiro
M
D003001:Cloning, Molecular; D003577:Cytochrome P-450 Enzyme System / Q000096:biosynthesis / Q000378:metabolism*; D015870:Gene Expression / Q000502:physiology*; D006900:Hydroxylation; D007850:Lauric Acids / Q000378:metabolism*; D030781:Organisms, Genetically Modified; D032306:Petunia / Q000201:enzymology*; D010940:Plant Proteins; D011994:Recombinant Proteins / Q000096:biosynthesis; D012441:Saccharomyces cerevisiae
D007850:Lauric Acids; D010940:Plant Proteins; D011994:Recombinant Proteins; C030358:lauric acid; D003577:Cytochrome P-450 Enzyme System