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Literature summary for 3.4.24.84 extracted from

  • Tam, A.; Schmidt, W.K.; Michaelis, S.
    The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor (2001), J. Biol. Chem., 276, 46798-46806.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
o-phenanthroline inhibition of recombinant Ste24 CAAX proteolytic activity Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
integral to membrane Ste24 has a lumenal N-terminus and a cytosolic C-terminus indicativ of an odd number of transmembrane spans, hydropathy analysis suggests 7 membrane spans Saccharomyces cerevisiae
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Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ restores Ste24 CAAX proteolytic activity after 1,10-phenanthroline treatment, reactivation with 0.25 mM Co2+ is 25% of that seen with 0.25 mM Zn2+ Saccharomyces cerevisiae
Zn2+
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Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged Ste24, nickel chelate chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
YIIKGVFWDPA(farnesyl)CVIA + H2O farnesylated 15-mer peptide containing the mature a-factor sequence and the native a-factor CAAX motif Saccharomyces cerevisiae YIIKGVFWDPA(farnesyl)C + Val-Ile-Ala
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