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ENZYME

ENZYME entry: EC 3.4.26.1

PURL: https://purl.expasy.org/enzyme/EC/3.4.26.1
Accepted Name
intramembrane prenyl-peptidase Rce1
Alternative Name(s)
CaaX prenyl protease 2
prenyl protein-specific endoprotease 2
Reaction catalysed
Hydrolyzes the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids with aliphatic sidechains and P3' is any C-terminal residue
Comment(s)
  • 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 homologs exist in humans and several other species.
  • Although the cleavage site is similar to that of the metallo- peptidase EC 3.4.24.84, there appear to be specificity differences in the proteins hydrolyzed by these two enzymes, with amino-acid substitution studies indicating activity of the yeast enzyme toward substrates with a hydrophilic residue at (P1') that are not hydrolyzed by EC 3.4.24.84.
Cross-references
BRENDA3.4.26.1
EC2PDB3.4.26.1
ExplorEnz3.4.26.1
KEGG Ligand Database for Enzyme Nomenclature3.4.26.1
IUBMB Enzyme Nomenclature3.4.26.1
MEDLINEFind literature relating to 3.4.26.1
MetaCyc3.4.26.1
Rhea expert-curated reactions3.4.26.1
UniProtKB/Swiss-Prot
Q8GW19, FACE2_ARATHA6H7A0, FACE2_BOVING5EEP3, FACE2_CAEEL
Q9U1H8, FACE2_DROMEQ9Y256, FACE2_HUMANP57791, FACE2_MOUSE
B0BMW8, FACE2_RATQ6LZY8, RCE1_METMPO94448, RCE1_SCHPO
Q03530, RCE1_YEAST

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