ExplorEnz: EC 2.3.2.23

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2.3.2.23

Accepted name:

E2 ubiquitin-conjugating enzyme

Reaction:

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine

Other name(s):

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

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.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	van Wijk, S.J. and Timmers, H.T. The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins. FASEB J. 24 (2010) 981–993. [DOI] [PMID: 19940261]
2.	David, Y., Ziv, T., Admon, A. and Navon, A. The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J. Biol. Chem. 285 (2010) 8595–8604. [DOI] [PMID: 20061386]
3.	Papaleo, E., Casiraghi, N., Arrigoni, A., Vanoni, M., Coccetti, P. and 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). [DOI] [PMID: 22815819]
4.	Cook, B.W. and Shaw, G.S. Architecture of the catalytic HPN motif is conserved in all E2 conjugating enzymes. Biochem. J. 445 (2012) 167–174. [DOI] [PMID: 22563859]
5.	Li, D.F., Feng, L., Hou, Y.J. and 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 (2013) 153–157. [DOI] [PMID: 23385757]

[EC 2.3.2.23 created 2015]