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

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.2.24
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RECOMMENDED NAME
GeneOntology No.
(E3-independent) E2 ubiquitin-conjugating enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-monoubiquitinyl-[(E3-independent) E2 ubiquitin-conjugating E2 enzyme]-L-cysteine + [acceptor protein]-L-lysine = [(E3-independent) E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-monoubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
(1b)
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [(E3-independent) E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-[(E3-independent) ubiquitin-conjugating enzyme]-L-cysteine
show the reaction diagram
(1a)
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-
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NIL
-
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protein ubiquitylation
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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].
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 N6-monoubiquitinyl-[Ubc1]-L-lysine
N6-diubiquitinyl-[Ubc1]-L-lysine + [Ube2K]-L-lysine
show the reaction diagram
-
-
-
?
2 N6-monoubiquitinyl-[Ube2K]-L-lysine
N6-diubiquitinyl-[Ube2K]-L-lysine + [Ube2K]-L-lysine
show the reaction diagram
-
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-L-lysine
show the reaction diagram
-
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)n-[E2 enzyme CDC34]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)(n+1)-[E2 enzyme CDC34]-L-lysine
show the reaction diagram
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CDC34 mutants differ in the extent of multiubiquitination they catalyze during an autoubiquitination reaction
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)n-[histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)(n+1)-[histone H2A]-L-lysine
show the reaction diagram
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reaction does not require additional factors such as E3 enzyme but depends on the E1 and ATP
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2g2-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2g2-L-cysteine
show the reaction diagram
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short chains of polyubiquitins can be linked bonds to E2 enzyme Ube2g2
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2K-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2K-L-cysteine
show the reaction diagram
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longer chains of polyubiquitins can be linked bonds to E2 enzyme Ube2K. Ubiquitin chains are assembled on the active site cysteine of Ube2K through thioester bond
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + UbcH10-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-UbcH10-L-cysteine
show the reaction diagram
-
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2g2-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2g2-L-cysteine
show the reaction diagram
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-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2K-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2K-L-cysteine
show the reaction diagram
-
-
-
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [cytochrome c]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[cytochrome c]-L-lysine lysine
show the reaction diagram
-
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approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 enzyme CDC34]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[E2 enzyme CDC34]-L-lysine
show the reaction diagram
-
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CDC34 mutants differ in the extent of multiubiquitination they catalyze during an autoubiquitination reaction
-
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H1]-L-lysine
show the reaction diagram
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significant rates of processive multiple ubiquitination of calf thymus H1 are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
show the reaction diagram
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine
show the reaction diagram
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine lysine
show the reaction diagram
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approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H3]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H3]-L-lysine
show the reaction diagram
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significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H4]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H4]-L-lysine
show the reaction diagram
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significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
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?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [alpha-casein]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [alpha-casein]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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42% relative activity compared to cytochrome c as substrate
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?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [alpha-lactalbumin]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [alpha-lactalbumin]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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12% with human and 15% with bovine alpha-lactalbumin, relative activity compared to cytochrome c as substrate
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?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [cytochrome c]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [cytochrome c]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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yeast cytochrome c, ubiquitin from human blood
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?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [histone H3]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [histone H3]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
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-
-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [lysozyme]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [lysozyme]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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5% relative activity compared to cytochrome c as substrate
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?
[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH2]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
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[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH2]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
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[ubiquitin-carrier protein UbcH5A]-S-ubiquitinyl-L-cysteine + [Stam2]-L-lysine
[ubiquitin-carrier protein UbcH5A]-L-cysteine + [Stam6]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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substrate protein Stam2 contains a N-terminal ubiquitin-interacting motif and VHS domain, it is most strongly ubiquitinated by E2 isoform UbcH5A
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[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
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[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
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[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol tau]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol tau]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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substrate protein Pol tau contains two C-terminal ubiquitin-associated domains. It is ubiquitinated by all E2 isoforms tested
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[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH6]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
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[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH6]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
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additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenite
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specific for vicinal sulfhydryl sites in proteins, irreversible or very slow reversible, instead of other inhibition with arsenite which is usually rapidly reversed upon addition of competitive dithiol compounds
casein
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71 microM inhibited by 50%, with 79 microM cytochrome c, competitive inhibition
iodoacetamide
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reacts slowly, relative insenstitive to iodoacetamide. This property distinguishes E2230K from other E2 proteins
lysozyme
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139 microM inhibited by 90%, with 79 microM cytochrome c, competitive inhibition
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additional information
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relatively insensitive to iodoacetamide inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.125
[cytochrome c]-L-lysine
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pH 7.0, 37°C, Vmax, 0.12 microM
0.00083 - 0.0028
[histone H2A]-L-lysine
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0.0015 - 0.012
[histone H2B]-L-lysine
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0.0013
[histone H3]-L-lysine
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pH 7.0, 37°C, Vmax, 0.06 microM
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00617
[cytochrome c]-L-lysine
Oryctolagus cuniculus
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pH 7.0, 37°C, Vmax, 0.12 microM
0.001 - 0.0013
[histone H2A]-L-lysine
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0.0022 - 0.0033
[histone H2B]-L-lysine
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0.003
[histone H3]-L-lysine
Oryctolagus cuniculus
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pH 7.0, 37°C, Vmax, 0.06 microM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.81
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pH 7.0, 37°C, purified enzyme, in the presence of 79 microM yeast cytochrome c and 0.1 microM E1 protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination; assay at, polyubiquitination
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17760
calculated
230000
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gel fitration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
E2 enzymes spontaneeously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin; E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin
monomer
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1 * 230000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification about 7fold with 20% recovery, gel filtration, ammonium sulfate fractionation, FPLC anion exchange on a Mono Q coloumn, E2230K is completely separated from other E2 proteins by the gel filtration step
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recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column; recombinant protein, Ni-NTA column
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; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag; expressed and transformed into Escherichia coli (BL-21 DE3) using pET22 vector in frame to a C-terminal His6 tag
expression in Escherichia coli