This title appears in the Scientific Report :
2021
Please use the identifier:
http://hdl.handle.net/2128/28510 in citations.
Please use the identifier: http://dx.doi.org/10.1515/hsz-2021-0166 in citations.
Glutamine synthetase as a central element in hepatic glutamine and ammonia metabolism: novel aspects
Glutamine synthetase as a central element in hepatic glutamine and ammonia metabolism: novel aspects
Glutamine synthetase (GS) in the liver is expressed in a small perivenous, highly specializedhepatocyte population and is essential for the maintenance of low, non‐toxic ammonia levelsin the organism. However, GS activity can be impaired by tyrosine nitration of the enzyme inresponse to oxidative/ni...
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Personal Name(s): | Frieg, Benedikt |
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Görg, Boris / Gohlke, Holger (Corresponding author) / Häussinger, Dieter (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; IBI-7 Jülich Supercomputing Center; JSC John von Neumann - Institut für Computing; NIC Bioinformatik; IBG-4 |
Published in: | Biological chemistry, 402 (2021) 9, S. 1063-1072 |
Imprint: |
Berlin [u.a.]
de Gruyter
2021
|
DOI: |
10.1515/hsz-2021-0166 |
PubMed ID: |
33962502 |
Document Type: |
Journal Article |
Research Program: |
Computational Science and Mathematical Methods Utilization of renewable carbon and energy sources and engineering of ecosystem functions Biological and environmental resources for sustainable use Domain-Specific Simulation & Data Life Cycle Labs (SDLs) and Research Groups |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1515/hsz-2021-0166 in citations.
Glutamine synthetase (GS) in the liver is expressed in a small perivenous, highly specializedhepatocyte population and is essential for the maintenance of low, non‐toxic ammonia levelsin the organism. However, GS activity can be impaired by tyrosine nitration of the enzyme inresponse to oxidative/nitrosative stress in a pH‐sensitive way. The underlying molecularmechanism as investigated by combined molecular simulations and in vitro experimentsindicates that tyrosine nitration can lead to a fully reversible and pH‐sensitive regulation ofprotein function. This approach was also used to understand the functional consequences ofseveral recently described point mutations of human GS with clinical relevance and to suggestan approach to restore impaired GS activity. |