Inhibitors | Comment | Organism | Structure |
---|---|---|---|
o-phenanthroline | - |
Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum | - |
Saccharomyces cerevisiae | 5783 | - |
integral to membrane | - |
Saccharomyces cerevisiae | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | - |
Homo sapiens | |
additional information | C-terminal proteolytic activity of Ste24 requires metall ions | Saccharomyces cerevisiae | |
Zn2+ | the in vitro N-terminal proteolysis of a-factor requires Zn2+ as metal cofactor, inhibition at higher Zn2+ concentrations e.g. 2 mM | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
a-factor + H2O | complements yeast ste24DELTA mutant | Homo sapiens | fragments of a-factor | - |
? | |
a-factor + H2O | Ste24 participates in both N- and C-terminal processing steps of a-factor | Homo sapiens | fragments of a-factor | - |
? | |
a-factor + H2O | Ste24 participates in both N- and C-terminal processing steps of a-factor | Saccharomyces cerevisiae | fragments of a-factor | - |
? | |
a-factor + H2O | mutant a-factor, containing a A8G point mutation is not cleaved suggesting that Ste24 N-terminal protease activity is highly discriminating | Saccharomyces cerevisiae | fragments of a-factor | - |
? |