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Literature summary for 3.4.24.84 extracted from

  • Schmidt, W.K.; Tam, A.; Michaelis, S.
    Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis (2000), J. Biol. Chem., 275, 6227-6233.
    View publication on PubMed
Search for more literature for 3.4.24.84

Inhibitors

Inhibitors Comment Organism Structure
o-phenanthroline
-
 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Saccharomyces cerevisiae 5783
-
integral to membrane
-
 Saccharomyces cerevisiae
-
-

Metals/Ions

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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

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
-
 ?