EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme

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IntEnz Enzyme Nomenclature
EC 2.3.2.23

Names

Accepted name:
E2 ubiquitin-conjugating enzyme
Other names:
ubiquitin-carrier-protein E2
UBC [ambiguous]
ubiquitin-conjugating enzyme E2
Systematic name:
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:[E2 ubiquitin-conjugating enzyme] ubiquitinyl transferase

Reaction

Comments:

The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage. Formerly EC 6.3.2.19.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (254) [show] [UniProt]

References

  1. van Wijk, S. J., Timmers, H. T.
    The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins.
    FASEB J. 24: 981-993 (2010). [PMID: 19940261]
  2. David, Y., Ziv, T., Admon, A., Navon, A.
    The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines.
    J. Biol. Chem. 285: 8595-8604 (2010). [PMID: 20061386]
  3. Papaleo, E., Casiraghi, N., Arrigoni, A., Vanoni, M., Coccetti, P., De Gioia, L.
    Loop 7 of E2 enzymes: an ancestral conserved functional motif involved in the E2-mediated steps of the ubiquitination cascade.
    PLoS ONE 7: e40786 (2012). [PMID: 22815819]
  4. Cook, B. W., Shaw, G. S.
    Architecture of the catalytic HPN motif is conserved in all E2 conjugating enzymes.
    Biochem. J. 445: 167-174 (2012). [PMID: 22563859]
  5. Li, D. F., Feng, L., Hou, Y. J., Liu, W.
    The expression, purification and crystallization of a ubiquitin-conjugating enzyme E2 from Agrocybe aegerita underscore the impact of His-tag location on recombinant protein properties.
    Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69: 153-157 (2013). [PMID: 23385757]

[EC 2.3.2.23 created 2015]