The Enzyme Database

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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]
[EC 6.3.2.19 created 1986]
 
 


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