EC Number   |
Substrates |
Products |
Reversibility |
|---|
   6.2.1.45 | more |
CDC42 is a substrate of UBA6-initiated ubiquitination |
? |
- |
? |
| 6.2.1.45 | more |
chimeric mutant Aos1-Uba2 SUMO-E1 enzyme shows SUMO-E1 activity. The E1 enzyme catalyzes the formation of a thioester-linked complex between SUMO and the E2 enzyme. This process is initiated by activation of the carboxyl terminus of SUMO by adenylation, followed by a thioesterification reaction in which SUMO is conjugated to a cysteine residue at the active site of Uba2 in the E1 enzyme. SUMO is then transferred to the active site cysteine of the E2 enzyme, Ubc9, via a trans-thioesterification reaction. A SUMO-charged E2 enzyme and substrate are finally bound with or without the assistance of a distinct class of SUMO E3-ligases, resulting in the activated SUMO bound to the substrate through an isopeptide linkage |
? |
- |
? |
| 6.2.1.45 | ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine |
E1 activates ubiquitin or an ubiquitin-like protein and transfers it to the E2-conjugating enzyme |
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine |
- |
? |
| 6.2.1.45 | more |
E1 activity is assesssed by the capacity of the enzyme to form a thiol ester conjugate with ubiquitin in an ATP-dependent process and to transfer this activated ubiquitin molecule to an conjugating enzyme |
? |
- |
? |
| 6.2.1.45 | more |
E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex |
? |
- |
? |
| 6.2.1.45 | more |
E1 ubiquitin-activating enzyme UBA6 is the only E1 enzyme that can activate both ubiquitin and ubiquitin-like protein HLA-F adjacent transcript 10 (FAT10). FAT10 consists of two ubiquitin-like domains with 29% and 36% identity to ubiquitin, respectively, that are separated by a short linker region |
? |
- |
? |
| 6.2.1.45 | ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine |
E1-activating enzyme activates ubiquitin via an adenylated intermediate and catalyzes its transfer to an E2 enzyme |
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine |
- |
? |
| 6.2.1.45 | ATP + Oregon Green-labeled ubiquitin + [ubiquitin-activating protein E1]-L-cysteine |
enzyme efficiently accepts ubiquitin substrate fluorescently labeled by Oregon Green |
AMP + diphosphate + [ubiquitin-activating protein E1]-S-(Oregon Green-labeled ubiquitinyl)-L-cysteine |
- |
? |
| 6.2.1.45 | ATP + ubiquitin + [ubiquitin-activating protein UBA1]-L-cysteine |
enzyme forms higher molecular mass intermediates with ubiquitin |
AMP + diphosphate + [ubiquitin-activating protein UBA1]-S-ubiquitinyl-L-cysteine |
the enzyme-ubiquitin intermediates dissociate in presence of 2-mercaptoethanol, indicating thiolester linkage |
? |
| 6.2.1.45 | ATP + ubiquitin + [ubiquitin-activating protein UBA2]-L-cysteine |
enzyme forms higher molecular mass intermediates with ubiquitin |
AMP + diphosphate + [ubiquitin-activating protein UBA2]-S-ubiquitinyl-L-cysteine |
the enzyme-ubiquitin intermediates dissociate in presence of 2-mercaptoethanol, indicating thiolester linkage |
? |
