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@ARTICLE{Becker:894606,
author = {Becker, Daniel and Bharatam, Prasad V. and Gohlke, Holger},
title = {{F}/{G} {R}egion {R}igidity is {I}nversely {C}orrelated to
{S}ubstrate {P}romiscuity of {H}uman {CYP} {I}soforms
{I}nvolved in {M}etabolism},
journal = {Journal of chemical information and modeling},
volume = {61},
number = {8},
issn = {1549-960X},
address = {Washington, DC},
publisher = {American Chemical Society},
reportid = {FZJ-2021-03307},
pages = {4023–4030},
year = {2021},
abstract = {Of 57 human cytochrome P450 (CYP) enzymes, 12 metabolize
$90\%$ of xenobiotics. To our knowledge, no study has
addressed the relation between enzyme dynamics and substrate
promiscuity for more than three CYPs. Here, we show by
constraint dilution simulations with the Constraint Network
Analysis for the 12 isoforms that structural rigidity of the
F/G region is significantly inversely correlated to the
enzymes’ substrate promiscuity. This highlights the
functional importance of structural dynamics of the
substrate tunnel.},
cin = {JSC / NIC / IBI-7 / IBG-4},
ddc = {540},
cid = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IBG-4-20200403},
pnm = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
(SDLs) and Research Groups (POF4-511) / 2171 - Biological
and environmental resources for sustainable use (POF4-217) /
2172 - Utilization of renewable carbon and energy sources
and engineering of ecosystem functions (POF4-217) /
Forschergruppe Gohlke $(hkf7_20200501)$},
pid = {G:(DE-HGF)POF4-5111 / G:(DE-HGF)POF4-2171 /
G:(DE-HGF)POF4-2172 / $G:(DE-Juel1)hkf7_20200501$},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:34370479},
UT = {WOS:000688241800027},
doi = {10.1021/acs.jcim.1c00558},
url = {https://juser.fz-juelich.de/record/894606},
}