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Computer modeling of enzyme catalysi...

Tang, Sishi.

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Computer modeling of enzyme catalysis and inhibition.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Computer modeling of enzyme catalysis and inhibition./
作者:	Tang, Sishi.
面頁冊數:	114 p.
附註:	Source: Masters Abstracts International, Volume: 45-03, page: 1475.
Contained By:	Masters Abstracts International45-03.
標題:	Health Sciences, Pharmacology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR21328
ISBN:	9780494213285

Computer modeling of enzyme catalysis and inhibition.
Tang, Sishi.

Computer modeling of enzyme catalysis and inhibition. - 114 p.

Source: Masters Abstracts International, Volume: 45-03, page: 1475.

Thesis (M.Sc.)--University of Toronto (Canada), 2006.

Computer modeling techniques have been extensively used to aid drug design via enzymatic reactions studies. Here we present the investigations of 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. We found that the proposed mechanisms are not feasible energetically. The catalytic site architecture and binding interactions of PKC isozymes alpha, beta and zeta were investigated, in the context of PKC-beta inhibitor, ruboxistaurin. Homology modeling and docking were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes, respectively. For the first time, specific interactions for ruboxistaurin that favor binding to PKC-beta were uncovered. A second binding site was discovered for PKC-zeta, which provides opportunity to design isozyme-specific inhibitors.

ISBN: 9780494213285Subjects--Topical Terms:

1017717
Health Sciences, Pharmacology.

Computer modeling of enzyme catalysis and inhibition.
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520 $a Computer modeling techniques have been extensively used to aid drug design via enzymatic reactions studies. Here we present the investigations of 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. We found that the proposed mechanisms are not feasible energetically. The catalytic site architecture and binding interactions of PKC isozymes alpha, beta and zeta were investigated, in the context of PKC-beta inhibitor, ruboxistaurin. Homology modeling and docking were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes, respectively. For the first time, specific interactions for ruboxistaurin that favor binding to PKC-beta were uncovered. A second binding site was discovered for PKC-zeta, which provides opportunity to design isozyme-specific inhibitors.
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