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Information on EC 3.4.26.1 - intramembrane prenyl-peptidase Rce1

for references in articles please use BRENDA:EC3.4.26.1

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IUBMB Comments

The cleavage site motif is typically referred to as CaaX, where the letter a represents any amino acid, rather than alanine, and X represents the C-terminal amino acid of the target protein. The enzyme has been found in the yeast Saccharomyces cerevisiae and homologues exist in humans and several other species. Although the cleavage site is similar to that of the metallo-peptidase Ste24 endopeptidase (EC 3.4.24.84), there appear to be specificity differences in the proteins hydrolysed by these two enzymes, with amino-acid substitution studies indicating activity of the yeast enzyme towards substrates with a hydrophylic residue at (P1′) that are not hydrolysed by EC 3.4.24.84 .

The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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Hydrolyses the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where where P1' and P2' are amino acids with aliphatic sidechains and P3' is any C-terminal residue.

Synonyms
alpha-factor-converting enzyme RCE1, CaaX prenyl protease, CaaX prenyl protease 2, CAAX protease, FACE-2, farnesylated-proteins converting enzyme-2, glutamic-type intramembrane endopeptidase Rce1, PPEP, PPSEP 2, prenyl protein-specific endoprotease, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolyses the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where where P1' and P2' are amino acids with aliphatic sidechains and P3' is any C-terminal residue.
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