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Information on EC 2.3.2.24 - (E3-independent) E2 ubiquitin-conjugating enzyme

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.24 (E3-independent) E2 ubiquitin-conjugating enzyme
IUBMB Comments
The enzyme transfers a single ubiquitin directly from an ubiquitinated E1 ubiquitin-activating enzyme to itself, and on to a lysine residue of the acceptor protein without involvement of E3 ubiquitin transferases (cf. EC 2.3.2.26, EC 2.3.2.27). It forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and Mg2+-ATP and catalyses the conjugation of ubiquitin to protein substrates, independently of E3. This transfer has only been observed with small proteins. In vitro a transfer to small acceptors (e.g. L-lysine, N-acetyl-L-lysine methyl ester) has been observed .
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This record set is specific for:
UNIPROT: Q13404
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine
+
[acceptor protein]-L-lysine
=
[E1 ubiquitin-activating enzyme]-L-cysteine
+
[acceptor protein]-N6-monoubiquitinyl-L-lysine
Synonyms
ube2o, e2-230k, e2-epf ubiquitin carrier protein, ubiquitin carrier protein e2, ubiquitin-conjugating enzyme e2 variant 1, ubiquitin-conjugating enzyme e2 n, ubiquitin-conjugating enzyme e2 c, ubiquitin-conjugating enzyme e2 e1, ubiquitin-conjugating enzyme e2 l3, ubiquitin-conjugating enzyme e2 variant 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ubiquitin-conjugating enzyme E2 variant 1
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
show the reaction diagram
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues, the latter described for this enzyme. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical polyubiquitin chains that are linked through Lys63
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:L-lysine ubiquitinyl transferase ([E3 ubiquitin transferase]-independent)
The enzyme transfers a single ubiquitin directly from an ubiquitinated E1 ubiquitin-activating enzyme to itself, and on to a lysine residue of the acceptor protein without involvement of E3 ubiquitin transferases (cf. EC 2.3.2.26, EC 2.3.2.27). It forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and Mg2+-ATP and catalyses the conjugation of ubiquitin to protein substrates, independently of E3. This transfer has only been observed with small proteins. In vitro a transfer to small acceptors (e.g. L-lysine, N-acetyl-L-lysine methyl ester) has been observed [1].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UB2V1_HUMAN
147
0
16495
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Homo sapiens, Homo sapiens (O00762), Homo sapiens (P49427), Homo sapiens (P49459), Homo sapiens (P51668), Homo sapiens (P51965), Homo sapiens (P60604), Homo sapiens (P61077), Homo sapiens (P61086), Homo sapiens (P61088), Homo sapiens (P62253), Homo sapiens (P62256), Homo sapiens (P62837), Homo sapiens (P63146), Homo sapiens (P68036), Homo sapiens (Q13404), Homo sapiens (Q15819), Homo sapiens (Q16763), Homo sapiens (Q712K3), Homo sapiens (Q8WVN8), Homo sapiens (Q969T4), Homo sapiens (Q96B02), Homo sapiens (Q96LR5), Homo sapiens (Q9NPD8), Homo sapiens (Q9Y2X8)
Manually annotated by BRENDA team