Reaction: Hydrolyses the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids with aliphatic side chains and P3' is any C-terminal residue.
Comments: The enzyme hydrolyses proteins that terminate with a CaaX motif in which C is an S-isoprenylated cysteine residue, a is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.The enzyme, which is the Type example of peptidase family M48, is one of two enzymes that can catalyse this processing step for mating a-factor in yeast. Subsequently, the S-isoprenylated cysteine residue that forms the new C-terminus is methyl-esterified and forms a hydrophobic membrane-anchor. Differs from EC 3.4.26.1, intramembrane prenyl-peptidase Rce1, in its catalytic mechanism and substrate preference.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 148463-92-7
References:
1. Fujimura-Kamada, K., Nouvet, F.J. and Michaelis, S. A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor. J. Cell Biol. 136 (1997) 271-285. [PMID: 9015299]
2. Tam, A., Schmidt, W.K. and Michaelis, S. The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor. J. Biol. Chem. 276 (2001) 46798-46806. [PMID: 11581258]