Ubiquitin-Activating Enzymes
"Ubiquitin-Activating Enzymes" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A class of enzymes that catalyzes the ATP-dependent formation of a thioester bond between itself and UBIQUITIN. It then transfers the activated ubiquitin to one of the UBIQUITIN-PROTEIN LIGASES.
| Descriptor ID |
D044764
|
| MeSH Number(s) |
D08.811.464.938.249
|
| Concept/Terms |
Ubiquitin-Activating Enzymes- Ubiquitin-Activating Enzymes
- Enzymes, Ubiquitin-Activating
- Ubiquitin Activating Enzymes
- Ubiquitination Activating Enzyme E1
- Ubiquitin-Activating Enzyme
- Enzyme, Ubiquitin-Activating
- Ubiquitin Activating Enzyme
- Ubiquitin-Activating Enzyme E1
- Enzyme E1, Ubiquitin-Activating
- Ubiquitin Activating Enzyme E1
|
Below are MeSH descriptors whose meaning is more general than "Ubiquitin-Activating Enzymes".
Below are MeSH descriptors whose meaning is more specific than "Ubiquitin-Activating Enzymes".
This graph shows the total number of publications written about "Ubiquitin-Activating Enzymes" by people in this website by year, and whether "Ubiquitin-Activating Enzymes" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2010 | 2 | 0 | 2 |
| 2017 | 2 | 0 | 2 |
| 2018 | 2 | 1 | 3 |
| 2019 | 1 | 1 | 2 |
| 2021 | 1 | 0 | 1 |
| 2022 | 1 | 0 | 1 |
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Below are the most recent publications written about "Ubiquitin-Activating Enzymes" by people in Profiles.
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Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6. Nat Commun. 2022 08 19; 13(1):4880.
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Crystal structures of an E1-E2-ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification. Nat Commun. 2021 04 22; 12(1):2370.
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Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34. Nat Commun. 2019 07 24; 10(1):3296.
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Structural basis for adenylation and thioester bond formation in the ubiquitin E1. Proc Natl Acad Sci U S A. 2019 07 30; 116(31):15475-15484.
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Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme. Nat Commun. 2018 12 04; 9(1):5145.
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UFM1-Activating Enzyme 5 (Uba5) Requires an Extension to Get the Job Done Right. J Mol Biol. 2019 02 01; 431(3):479-482.
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Crystal structure of a human ubiquitin E1-ubiquitin complex reveals conserved functional elements essential for activity. J Biol Chem. 2018 11 23; 293(47):18337-18352.
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Domain alternation and active site remodeling are conserved structural features of ubiquitin E1. J Biol Chem. 2017 07 21; 292(29):12089-12099.
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S.?pombe Uba1-Ubc15 Structure Reveals a Novel Regulatory Mechanism of Ubiquitin E2 Activity. Mol Cell. 2017 Feb 16; 65(4):699-714.e6.
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Active site remodelling accompanies thioester bond formation in the SUMO E1. Nature. 2010 Feb 18; 463(7283):906-12.