Exploring Reaction Pathways for O-GlcNAc Transferase Catalysis. A String Method Study
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00085002" target="_blank" >RIV/00216224:14740/15:00085002 - isvavai.cz</a>
Result on the web
<a href="http://pubs.acs.org/doi/pdf/10.1021/jp511235f" target="_blank" >http://pubs.acs.org/doi/pdf/10.1021/jp511235f</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/jp511235f" target="_blank" >10.1021/jp511235f</a>
Alternative languages
Result language
angličtina
Original language name
Exploring Reaction Pathways for O-GlcNAc Transferase Catalysis. A String Method Study
Original language description
The inverting O-GlcNAc glycosyltransferase (OGT) is an important post-translation enzyme, which catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine (UDP-GlcNAc) to the hydroxyl group of the Ser/Thr of cytoplasmic, nuclear, and mitochondrial proteins. In the past, three different catalytic bases were proposed for the reaction: His498, alpha-phosphate, and Asp554. In this study, we used hybrid quantum mechanics/molecular mechanics (QM/MM) Car-Parrinello molecular dynamics to investigate reaction paths using alpha-phosphate and Asp554 as the catalytic bases. The string method was used to calculate the free-energy reaction profiles of the tested mechanisms. During the investigations, an additional mechanism was observed. In this mechanism, a proton is transferred to alpha-phosphate via a water molecule. Our calculations show that the mechanism with alpha-phosphate acting as the base is favorable. This reaction has a rate-limiting free-energy barrier of 23.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Physical Chemistry B
ISSN
1520-6106
e-ISSN
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Volume of the periodical
119
Issue of the periodical within the volume
12
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
4371-4381
UT code for WoS article
000351971100004
EID of the result in the Scopus database
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