Fusarium oxysporum fatty acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3

doi:10.1074/jbc.M005617200

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Papers In Press, published online ahead of print September 19, 2000
J. Biol. Chem, 10.1074/jbc.M005617200
Submitted on June 27, 2000
Revised on September 13, 2000
Accepted on September 18, 2000

Fusarium oxysporum fatty acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3

Tatsuya Kitazume, Naoki Takaya, Norikazu Nakayama, and Hirofumi Shoun

Applied Biochemistry, Tsukuba, Ibraki 305-8572

Corresponding Author: p450nor{at}sakura.cc.tsukuba.ac.jp

The gene of a fatty acid hydroxylase of the fungus Fusarium oxysporum (P450foxy) was cloned and expressed in the yeast. The putative primary structure revealed the close relationship of P450foxy to the bacterial cytochrome P450BM3, a fused protein of cytochrome P450 (P450) and its reductase from Bacillus megaterium. The amino acid sequence identities of the P450 and P450 reductase domains of P450foxy were highest (40.6% and 35.3%, respectively) to the corresponding domains of P450BM3. The recombinant protein (rP450foxy) expressed in the yeast was catalytically and spectrally indistinguishable from the native protein, whereas most rP450foxy was recovered in the soluble fraction of the yeast cells in marked contrast to native P450foxy, which was exclusively recovered in the membrane fraction of the fungal cells. This difference implies that a post- (or co-) translational mechanism functions in the fungal cells to target and bind the protein to the membrane. These results provided conclusive evidence that P450foxy is the eukaryotic counterpart of bacterial P450BM3, which evokes interest in the evolutionary aspects of concerning the P450 superfamily along with its reducing systems. P450foxy was classified into the new family, CYP505.

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