| Ubiquitin-activating enzymes | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure of the yeast ubiquitin-activating enzyme E1 / ubiquitin complex.[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 6.2.1.45 | ||||||||
| CAS no. | 74812-49-0 | ||||||||
| Alt. names | E1 enzymes | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Ubiquitin-activating enzymes, also known as E1 enzymes, catalyze the first step in the ubiquitination reaction, which (among other things) can target a protein for degradation via a proteasome. This covalent bond of ubiquitin or ubiquitin-like proteins to targeted proteins is a major mechanism for regulating protein function in eukaryotic organisms.[2] Many processes such as cell division, immune responses and embryonic development are also regulated by post-translational modification by ubiquitin and ubiquitin-like proteins.[2]
- ^ PDB: 3CMM; Lee I, Schindelin H (July 2008). "Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes". Cell. 134 (2): 268–78. doi:10.1016/j.cell.2008.05.046. PMID 18662542.
- ^ a b Schulman BA, Harper JW (May 2009). "Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways". Nature Reviews Molecular Cell Biology. 10 (5): 319–31. doi:10.1038/nrm2673. PMC 2712597. PMID 19352404.