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Journal of Virology, August 2009, p. 8266-8269, Vol. 83, No. 16
0022-538X/09/$08.00+0 doi:10.1128/JVI.00289-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Institute of Life Science and School of Medicine, Swansea University, Swansea SA2 8PP, United Kingdom,1 Department of Biochemistry,2 Center for Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 372323
Received 10 February 2009/ Accepted 2 June 2009
The genome sequence of the giant virus Acanthamoeba polyphaga mimivirus revealed the presence of two putative cytochrome P450 (CYP) genes. The product of one of the two predicted CYP genes (YP_143162) showed low-level homology to sterol 14-demethylase (CYP51) and contained a C-terminal polypeptide domain of unknown function. YP_143162 expression (without an N-terminal membrane binding domain) in Escherichia coli yields a CYP protein which gives a reduced CO difference maximum at 448 nm and was formally demonstrated as the first viral cytochrome P450. Analysis of binding of lipid and sterol substrates indicated no perturbation in CYP heme environment, and an absence of activity was seen when 14-methyl sterols were used as a substrate. The function of the CYP protein and its C-terminal domain remain unknown.
Published ahead of print on 10 June 2009.
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