Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of chimeric protein substrates: 1. the matrix domain of Yme2p is replaced by mouse dihydrofolate reductase, 2. a chimeric protein consisting of a loosely folded mutant variant of dihydrofolate reductase and the C-terminal end of Yme2p | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrial inner membrane | - |
Saccharomyces cerevisiae | 5743 | - |
mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protein + H2O | Saccharomyces cerevisiae | degradation of proteins exposing loops or domain at either sides of the mitochondrial inner membrane | peptides | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
proteolytic degradation of proteins | overlapping substrate specificity with i-AAA protease EC 3.4.24.B19, mechanism, reaction involves an active extraction of transmembrane segments and transport of solvent-exposed domains across the membrane, inner membrane proteins, active site at the opposite membrane surface | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
mitochondrial integral inner membrane protein Yme2p + H2O | wild-type and chimeric mutant containing the dihydrofolate reductase loosely folded mutant, not the one containing the wild-type dihydrofolate reductase, overview, unfolding of the substrate at one side of the membrane might be sufficient for proteolysis, in vitro synthesized protein substrate, imported into the mitochondria, spans the membrane once and exposes large domains at both membrane surfaces | Saccharomyces cerevisiae | ? | - |
? | |
additional information | construction of several deletion mutants of Yme2p and investigation of their behaviour as substrates, overview, the folded intermembrane space domain of Yme2p prevents proteolysis but not protease binding at the opposite membrane side | Saccharomyces cerevisiae | ? | - |
? | |
protein + H2O | degradation of proteins exposing loops or domain at either sides of the mitochondrial inner membrane | Saccharomyces cerevisiae | peptides | - |
? |
Synonyms | Comment | Organism |
---|---|---|
M41.003 | Merops-ID | Saccharomyces cerevisiae |
mitochondrial AAA protease | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Saccharomyces cerevisiae |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
no activity at 25°C, unfolding of Yme2p at 37°C triggers its proteolytic breakdown | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on | Saccharomyces cerevisiae |