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A more recent version of this article appeared on November 27, 2002
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277/49/46959    most recent
M203523200v1
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Papers In Press, published online ahead of print September 13, 2002
J. Biol. Chem, 10.1074/jbc.M203523200
Submitted on April 11, 2002
Revised on September 11, 2002
Accepted on September 13, 2002

A novel sterol 14alpha -demethylase/ferredoxin fusion protein (MCCYP51FX) from methylococcus capsulatus represents a new class of the cytochrome P450 superfamily

Colin J. Jackson, David C. Lamb, Timothy Marczylo, Andrew G. S. Warrilow, Nigel J. Manning, David J. Lowe, Diane E. Kelly, and Steven L. Kelly

Biological Sciences, University of Wales Aberystwyth, Aberystwyth SY23 3DA

Corresponding Author: david.lamb{at}toxicology.mc.vanderbilt.edu

Sterol 14-demethylase encoded by CYP51 is a member of the cytochrome P450 (CYP) superfamily of enzymes and has been shown to have an essential role in sterol biosynthesis in eukaryotes, with orthologues recently being described in some bacteria. Examination of the genome sequence data for the proteobacterium Methylococcus capsulatus, a bacterial species known to produce sterol, revealed the presence of a single CYP with strong homology to CYP51, particularly to a form in Mycobacterium tuberculosis. Interestingly, this M. capsulatus CYP51 protein represents a new class of CYP consisting of the CYP domain naturally fused to a ferredoxin domain at the C-terminus via an alanine rich linker. Expression of the M. capsulatus MCCYP51FX fusion in Escherichia coli yields a P450, which, when purified to homogeneity, has the predicted molecular mass ca 62kDa on SDS/PAGE and bound lanosterol as a putative substrate. Activity in sterol 14a-demethylase activity was shown (0.24 nmol lanosterol metabolised/min/nmol MCCYP51FX fusion) by GC/MS with the activity dependent upon the presence of ferredoxin reductase and NADPH. Our unique findings describe a new class of naturally existing cytochrome P450, which will provide pivotal information for CYP structure/function in general.


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