SUMO activating enzyme activity

Definition

Target type: molecularfunction

Catalysis of the activation of the proteolytically processed small ubiquitin-related modifier SUMO, through the formation of an ATP-dependent high-energy thiolester bond. [GOC:rn, PMID:10187858, PMID:11265250]

SUMO activating enzyme activity, also known as E1 activity, is a crucial step in the SUMOylation pathway, a post-translational modification process that involves the covalent attachment of small ubiquitin-like modifier (SUMO) proteins to target proteins. The SUMO activating enzyme (SAE1/SAE2 heterodimer) catalyzes a two-step reaction that ultimately activates SUMO for conjugation:

1. **SUMO Adenylation:** The SAE1/SAE2 heterodimer binds to SUMO and uses ATP to adenylate the SUMO C-terminus, forming a SUMO-adenylate intermediate.
2. **SUMO Thioesterification:** The adenylated SUMO is then transferred to a cysteine residue on the SAE2 subunit, forming a SUMO-SAE2 thioester bond. This activated SUMO molecule is now primed for conjugation to target proteins.

The SUMO activating enzyme activity is essential for the proper functioning of the SUMOylation pathway, which plays a vital role in various cellular processes, including protein trafficking, DNA repair, signal transduction, and transcriptional regulation. Dysregulation of SUMO activating enzyme activity can lead to various diseases, including cancer and neurodegenerative disorders.'
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Proteins (4)

Compounds (4)