EC Number   |
Substrates |
Products  |
Reversibility |
|---|
   6.2.1.45 | more |
kinetics for Uba1a-catalyzed transthiolation of Ubc2b are used as a reporter assay for determining the Km and kcat values for the three cosubstrates of the ubiquitin-activating enzyme. The E2 transthiolation assays are more sensitive to the potential presence of trace catalytically active fragments than the single turnover end point assays used for quantitating ternary complex stoichiometry |
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| 6.2.1.45 | more |
purified isoform UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL |
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| 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 |
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| 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 |
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| 6.2.1.45 | more |
orthogonal ubiquitin transfer (OUT) technology to profile their ubiquitination targets in mammalian cells of isozymes Uba1 and Uba6 |
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| 6.2.1.45 | more |
the non-canonical E1, UBA5, binds to the ubiquitin-like protein UFM1 using a trans-binding mechanism in which UFM1 interacts with distinct sites in both subunits of the UBA5 dimer. Mechanism of UFM1 activation by UBA5 and trans-binding mechanism of UFM1 transfer to the E2, UFC1. UFM1 contains a C-terminal Val-Gly dipeptide instead of the canonical Gly-Gly dipeptide present in ubiquitin and other ubiquitin-like proteins |
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| 6.2.1.45 | more |
CDC42 is a substrate of UBA6-initiated ubiquitination |
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| 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 |
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? |
| 6.2.1.45 | ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine |
- |
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine |
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? |
| 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 |
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