EC Number | Cloned (Comment) | Organism |
---|---|---|
6.2.1.45 | recombinant expression of His6-tagged chimeric mutant Aos1-Uba2 SUMO-E1 enzyme mAU in Spodoptera frugiperda Sf9 insect cells via baculovirus transformation, mAU has SUMO-E1 activity. Recombinant expression of GST-tagged mAU in Escherichia coli | Mus musculus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
6.2.1.45 | additional information | construction of a mouse Aos1-Uba2 chimeric SUMO(small ubiquitin-related modifier)-E1 enzyme, mAU. The SUMO-E1 enzyme consists of two subunits, a heterodimer of activation of Smt3p 1 (Aos1) and ubiquitin activating enzyme 2 (Uba2), which resembles the N- and C-terminal halves of ubiquitin E1 (Uba1), the functional domains appear to be arranged in a fashion similar to Uba1. mAU has SUMO-E1 activity, indicating that mAU can be expressed in baculovirus-insect cells and represents a suitable source of SUMO-E1, enzymatic mechanism and structure of SUMO-E1, overview | Mus musculus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.45 | Mg2+ | required | Mus musculus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
6.2.1.45 | 130000 | - |
recombinant His6-tagged chimeric mutant Aos1-Uba2 SUMO-E1 enzyme mAU, gel filtration | Mus musculus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.45 | ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine | Mus musculus | - |
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.2.1.45 | Mus musculus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.2.1.45 | recombinant His-tagged chimeric mutant Aos1-Uba2 SUMO-E1 enzyme mAU from insect cells by nickel affinity chromatography | Mus musculus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.45 | ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine | - |
Mus musculus | AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine | - |
? | |
6.2.1.45 | additional information | 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 | Mus musculus | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.2.1.45 | UBA2 | - |
Mus musculus |
6.2.1.45 | ubiquitin activating enzyme 2 | - |
Mus musculus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.45 | ATP | - |
Mus musculus |