Phanerochaete chrysosporium i
s widely u
sed a
s a model organi
sm to under
stand the phy
siology, enzymology, and genetic
s of lignin degradation by white rot fungi and i
s known for it
s ability to metabolize and detoxify a wide range of environmental chemical
s. Our pre-genomic effort
s and the recent whole genome
sequencing by the Joint Genome In
stitute of the US-DOE have revealed that thi
s fungu
s carrie
s a well-developed P450 enzyme
sy
stem, con
si
sting of multiple P450 monooxygena
se
s and a common P450 oxidoreducta
se. The entire P450ome of thi
s organi
sm compri
se
s of
![]()
src=""http://www.
sciencedirect.com/
scidirimg/entitie
s/223c.gif"" alt=""not, vert,
similar"" title=""not, vert,
similar"" border=""0"">150 cytochrome P450 monooxygena
se
s, mo
stly arranged in gene clu
ster
s and cla
ssifiable into multigene familie
s. Except for the
structurally and functionally con
served fungal P450 familie
s such a
s CYP51, CYP61, and CYP53, other P450 enzyme
s in thi
s organi
sm have largely unknown function and will require functional characterization. The
se new P450 enzyme
s may likely have role
s in biodegradation activity and phy
siology of thi
s ligninolytic fungu
s. Our pre- and po
st-genomic effort
s to under
stand the functional role of P450 enzyme
sy
stem
s in
P. chrysosporium have focu
sed on the regulation of expre
ssion of the fir
st identified family of P450 enzyme
s, the CYP63 family, and genome-wide regulation of the other P450 familie
s u
sing a cu
stom-de
signed P450 microarray. The genomically linked CYP63 member P450
s were found to be differentially regulated under varying phy
siological and/or biodegradation condition
s. Re
sult
s on the heterologou
s expre
ssion of thi
s family of monooxygena
se
s in different prokaryotic and eukaryotic expre
ssion
sy
stem
s are pre
sented and the inherent problem
s a
ssociated with the expre
ssion of the
se membrane protein
s are di
scu
ssed. Further, we report the expre
ssion and purification of the white rot fungal cytochrome P450 oxidoreducta
se (POR), the electron tran
sfer component of it
s P450 enzyme
sy
stem, required for P450 cataly
si
s. The reported
studie
s have uncovered the hitherto unknown regulatory a
spect
s of the P450 enzyme
sy
stem in
P. chrysosporium and generated u
seful expre
ssion tool
s and knowledge ba
se to pur
sue further
studie
s on functional analy
si
s of the P450 contingent in thi
s model white rot fungu
s.