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J. Biol. Chem., Vol. 275, Issue 50, 39734-39740, December 15, 2000
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From the Institute of Applied Biochemistry, University of Tsukuba,
Tsukuba, Ibaraki 305-8572, Japan
The gene of a fatty-acid hydroxylase of the
fungus Fusarium oxysporum (P450foxy) was cloned and
expressed in yeast. The putative primary structure revealed the close
relationship of P450foxy to the bacterial cytochrome P450BM3, a fused
protein of cytochrome 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. Recombinant
P450foxy expressed in yeast was catalytically and spectrally
indistinguishable from the native protein, except most of the
recombinant P450foxy 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 provide conclusive evidence that P450foxy is the eukaryotic
counterpart of bacterial P450BM3, which evokes interest in the
evolutionary aspects concerning the P450 superfamily along with its
reducing systems. P450foxy was classified in the new family, CYP505.
The nucleotide sequence reported in this paper has been submitted
to the DDBJ/GenBankTM/EBI Data Bank with
accession number AB030037.
Fusarium oxysporum Fatty-acid Subterminal
Hydroxylase (CYP505) Is a Membrane-bound Eukaryotic Counterpart
of Bacillus megaterium Cytochrome P450BM3*
, and
*
This work was supported by PROBRAIN (Program for Promotion
of Basic Research Activities for Innovative Biosciences); a
grant-in-aid for scientific research from the Ministry of Education,
Science, Culture, and Sports of Japan; and the Sakabe Project (High
Energy Accelerator Research Organization, Tsukuba, Japan).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Legume Physiology Laboratory, National
Agriculture Research Center, Tsukuba, Ibaraki 305-8666, Japan.
§
To whom correspondence should be addressed. Tel.: 81-298-53-4603;
Fax: 81-298-53-4605; E-mail: p450nor@sakura.cc.tsukuba.ac.jp.
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