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Literature summary for 3.4.22.68 extracted from
- Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast (2000), Mol. Cell, 5, 865-876.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| Ulp1-Smt3 crystal structure, hanging drop vapor diffusion | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| SUMO-1 protein + H2O | Saccharomyces cerevisiae | Ulp1 catalyzes two essential functions in the SUMO pathway: 1. the processing of full-length SUMO to its mature form and 2. deconjugation of SUMO from target proteins. Ulp1 can proteolyze large folded SUMO-conjugated proteins without altering their structure | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | Q02724 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| SUMO-1 protein + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
| SUMO-1 protein + H2O | Ulp1 catalyzes two essential functions in the SUMO pathway: 1. the processing of full-length SUMO to its mature form and 2. deconjugation of SUMO from target proteins. Ulp1 can proteolyze large folded SUMO-conjugated proteins without altering their structure | Saccharomyces cerevisiae | ? | - |
? | |
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