Conjugation of SUMO1 to UBA2:SAE1

Stable Identifier
Reaction [transition]
Homo sapiens
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The UBA2:SAE1 complex catalyzes the formation of a thioester bond between SUMO1 and cysteine-173 of UBA2 (Desterro et al. 1999, Okuma et al. 1999, Werner et al. 2009, Olsen et al. 2010, Wang and Chen 2010). ATP reacts with the C-terminal glycine residue of SUMO1 to yield pyrophosphate and a transient intermediate, SUMO1 adenylate, which then reacts with the thiol group of the cysteine residue on UBA2.
Literature References
PubMed ID Title Journal Year
9920803 In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2

Yasuda, H, Honda, R, Tsumagari, N, Ichikawa, G, Okuma, T

Biochem. Biophys. Res. Commun. 1999
10187858 Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1

Desterro, JM, Kemp, GD, Rodriguez, MS, Hay, RT

J. Biol. Chem. 1999
19107418 Performing in vitro sumoylation reactions using recombinant enzymes

Moutty, MC, Melchior, F, Möller, U, Werner, A

Methods Mol. Biol. 2009
20164921 Active site remodelling accompanies thioester bond formation in the SUMO E1

Capili, AD, Lu, X, Olsen, SK, Lima, CD, Tan, DS

Nature 2010
20501649 Role of the Zn(2+) motif of E1 in SUMO adenylation

Wang, J, Chen, Y

J. Biol. Chem. 2010
Catalyst Activity

SUMO activating enzyme activity of UBA2:SAE1 [nucleoplasm]

Orthologous Events
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