Computational Study of the MutH Enzyme Reactivity
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F10%3A00049618" target="_blank" >RIV/00216224:14310/10:00049618 - isvavai.cz</a>
Výsledek na webu
—
DOI - Digital Object Identifier
—
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Computational Study of the MutH Enzyme Reactivity
Popis výsledku v původním jazyce
MutH enzyme is an integral part of the DNA repair mechanism called Methyl-directed Mismatch Repair, which is responsible for removing of mismatches introduced in DNA replication process. The repair mechanism depends on three enzymes MutS, MutL and MutH which cooperate on following way: the mismatch is identified by MutS and the information is transferred through MutL to MutH enzyme, which specifically recognizes GATC sequence on daughter DNA strand. Close to the G base this strand is cleaved by MutH andincorrectly paired base is removed. Missing part of DNA can be renewed. Here we present the elucidation of the MutH enzyme reaction mechanism using computational chemistry approach, namely Quantum Mechanics/Molecular Mechanics (QM/MM) tools. All available structures are considered as the pre-reaction complexes because they contain Ca2+ ions which inhibit the cleavage reaction. To suggest the reaction mechanism of the cleavage, the Mg2+ (known as cofactors) are included to the calculatio
Název v anglickém jazyce
Computational Study of the MutH Enzyme Reactivity
Popis výsledku anglicky
MutH enzyme is an integral part of the DNA repair mechanism called Methyl-directed Mismatch Repair, which is responsible for removing of mismatches introduced in DNA replication process. The repair mechanism depends on three enzymes MutS, MutL and MutH which cooperate on following way: the mismatch is identified by MutS and the information is transferred through MutL to MutH enzyme, which specifically recognizes GATC sequence on daughter DNA strand. Close to the G base this strand is cleaved by MutH andincorrectly paired base is removed. Missing part of DNA can be renewed. Here we present the elucidation of the MutH enzyme reaction mechanism using computational chemistry approach, namely Quantum Mechanics/Molecular Mechanics (QM/MM) tools. All available structures are considered as the pre-reaction complexes because they contain Ca2+ ions which inhibit the cleavage reaction. To suggest the reaction mechanism of the cleavage, the Mg2+ (known as cofactors) are included to the calculatio
Klasifikace
Druh
O - Ostatní výsledky
CEP obor
CE - Biochemie
OECD FORD obor
—
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Ostatní
Rok uplatnění
2010
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů