Computer Modeling of Enzyme Catalysis and Inhibition
A Study on ODCase Catalysis and Protein Kinase C
Inhibition
978-3-639-12501-6
3639125010
92
2009-04-03
49.00 €
eng
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Computer modeling techniques have been extensively
used to aid drug design via enzymatic reaction
studies. Here we present the investigations of the
catalysis by orotidine monophosphate decarboxylase
(ODCase) and the inhibition of protein kinase C
(PKC) isozymes. Decarboxylation, pseudohydrolysis
and covalent inhibition reactions were studied using
QM and QM/MM methods to understand the mechanistic
details of ODCase catalysis. The catalytic site
architecture and binding interactions of PKC
isozymes α, β and ζ were also investigated in the
context of PKC-β inhibitor, ruboxistaurin. Homology
modeling and docking techniques were used to model
the three-dimensional structures of the kinase
domains of PKC isozymes and the PKC-ruboxistaurin
complexes. For the first time, specific interactions
for ruboxistaurin that favor binding to PKC-β were
uncovered. Our study provides opportunity to design
isozyme-specific inhibitors for PKC.
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