Target type: molecularfunction
An thiol-dependent isopeptidase activity that cleaves SUMO from a target protein to which it is conjugated. [GOC:rn, PMID:10094048, PMID:11031248, PMID:11265250, PMID:23746258]
DeSUMOylase activity is a molecular function associated with enzymes that specifically remove SUMO (Small Ubiquitin-like Modifier) proteins from target proteins. SUMOylation, the process of attaching SUMO proteins to target proteins, is a post-translational modification that can alter the function, localization, and stability of the target protein. DeSUMOylation, conversely, acts as a dynamic counterbalance to SUMOylation, regulating the overall SUMOylation state of a protein and influencing its cellular activity.
DeSUMOylase enzymes employ a catalytic mechanism involving the cleavage of the isopeptide bond between the C-terminal Glycine residue of SUMO and the Lysine residue on the target protein. This process is typically achieved through a two-step mechanism:
1. **Binding:** DeSUMOylase enzymes first recognize and bind to the SUMO-modified target protein, often through specific protein-protein interactions involving the SUMO moiety and the deSUMOylase active site.
2. **Cleavage:** The bound deSUMOylase then utilizes its catalytic activity to cleave the isopeptide bond between SUMO and the target protein, releasing the SUMO moiety and restoring the unmodified form of the target protein.
DeSUMOylase activity is crucial for a wide range of cellular processes, including:
- **Transcriptional Regulation:** DeSUMOylation can modulate the activity of transcription factors, influencing gene expression and cellular responses.
- **Signal Transduction:** DeSUMOylation can regulate the activity of signaling proteins, influencing cellular communication and responses to external stimuli.
- **Protein Stability and Degradation:** DeSUMOylation can influence protein stability and degradation pathways, affecting the cellular proteome.
- **Cellular Stress Responses:** DeSUMOylation plays a role in cellular responses to stress, including DNA damage and oxidative stress.
Overall, deSUMOylase activity represents a critical regulatory mechanism in cells, allowing for the dynamic control of protein function and cellular processes through the removal of SUMO modifications.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Sentrin-specific protease 2 | A sentrin-specific protease 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9HC62] | Homo sapiens (human) |
| Sentrin-specific protease 1 | A sentrin-specific protease 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9P0U3] | Homo sapiens (human) |
| Histidine triad nucleotide-binding protein 1 | An adenosine 5-monophosphoramidase HINT1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P49773] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| streptonigrin | pyridines; quinolone | antimicrobial agent; antineoplastic agent | |
| ursolic acid | hydroxy monocarboxylic acid; pentacyclic triterpenoid | geroprotector; plant metabolite | |
| Tormentic acid | tormentic acid: aglycone of Rosamultin | triterpenoid | metabolite |
| atromentin | atromentin : A member of the class of dihydroxy-1,4-benzoquinones that is 2,5-dihydroxycyclohexa-2,5-diene-1,4-dione which is substituted by a 4-hydroxyphenyl group at positions 3 and 6. It is a mushroom pigment isolated from several fungi species and acts as a smooth muscle stimulant, and exhibits anticoagulant, antibacterial and antineoplastic properties. atromentin: an enoyl-ACP reductase (FabK) inhibitor; isolated from Streptococcus pneumoniae; structure in first source | dihydroxy-1,4-benzoquinones; polyphenol | antibacterial agent; anticoagulant; antineoplastic agent; apoptosis inducer; biological pigment; EC 1.3.1.9 [enoyl-[acyl-carrier-protein] reductase (NADH)] inhibitor; fungal metabolite |
| scoparianoside b | scoparianoside B: isolated from the fruit of Japanese Kochia scoparia; structure given in first source | triterpenoid saponin | |
| pomolic acid | pomolic acid: from Rosa woodsii & Hyptis capitata; structure in first source | triterpenoid | metabolite |
| vialinin a | vialinin A: free radical scavenger from an edible mushroom in China; structure in first source | ||
| gn6958 | GN6958: inhibits SUMO-sentrin specific protease 1 (SENP1); structure in first source | ||
| guanosine monophosphate | guanosine 5'-monophosphate : A purine ribonucleoside 5'-monophosphate having guanine as the nucleobase. Guanosine Monophosphate: A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature. | guanosine 5'-phosphate; purine ribonucleoside 5'-monophosphate | biomarker; Escherichia coli metabolite; metabolite; mouse metabolite |