| EC |
6.3.2.19 |
| Accepted name: |
ubiquitin—protein ligase |
| Reaction: |
ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine |
| Other name(s): |
ubiquitin-activating enzyme |
| Systematic name: |
ubiquitin:protein-lysine N-ligase (AMP-forming) |
| Comments: |
Ubiquitin is coupled to protein by a peptide bond between the C-terminal glycine of ubiquitin and ε-amino groups of lysine residues in the protein. An intermediate in the reaction contains one ubiquitin residue bound as a thioester to the enzyme, and a residue of ubiquitin adenylate non-covalently bound to the enzyme. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, METACYC, PDB, CAS registry number: 74812-49-0 |
| References: |
| 1. |
Ciechanover, A., Elias, S., Heller, H. and Hershko, A. Covalent affinity purification of ubiquitin-activating enzyme. J. Biol. Chem. 257 (1982) 2537–2542. [PMID: 6277904] |
| 2. |
Haas, A.L. and Rose, I.A. The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. J. Biol. Chem. 257 (1982) 10329–10337. [PMID: 6286650] |
| 3. |
Haas, A.L., Warms, J.V.B., Hershko, A. and Rose, I.A. Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem. 257 (1982) 2543–2548. [PMID: 6277905] |
| 4. |
Hershko, A., Heller, H., Eytan, E. and Reiss, Y. The protein substrate binding site of the ubiquitin-protein ligase system. J. Biol. Chem. 261 (1986) 11992–11999. [PMID: 3017957] |
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| [EC 6.3.2.19 created 1986] |
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