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Literature summary for 3.4.24.B19 extracted from
- A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space (2006), Mol. Cell. Biol., 26, 8488-8497.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | polynucleotide phosphorylase-dihydrofolate reductase is not a proteolytic substrate for Yme1 | Saccharomyces cerevisiae | ? | - |
? |  |
| polynucleotide phosphorylase + H2O | Yme1 is required for PNPase assembly in the intermembrane space | Saccharomyces cerevisiae | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| YME1 | - |
Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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