Theoretical study on the catalytic mechanism of human deoxyhypusine hydroxylase
Author:
Affiliation:
1. Key Laboratory of Theoretical and Computational Photochemistry
2. College of Chemistry
3. Beijing Normal University
4. Beijing 100875
5. China
Abstract
Deoxyhypusine hydroxylase is a critical enzyme for hypusination of eukaryotic translation initiation factor 5A.
Funder
National Natural Science Foundation of China
National Basic Research Program of China
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2020/CP/D0CP03598J
Reference48 articles.
1. Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification
2. The unique hypusine modification of eIF5A promotes islet β cell inflammation and dysfunction in mice
3. Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.
4. Modification of eukaryotic initiation factor 5A from Plasmodium vivax by a truncated deoxyhypusine synthase from Plasmodium falciparum: An enzyme with dual enzymatic properties
5. In vivo tumor suppression activity by T cell-specific T-bet restoration
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