CATH Classification

Domain Context

CATH Clusters

Superfamily Metalloproteases ("zincins"), catalytic domain
Functional Family CAAX prenyl protease

Enzyme Information

3.4.24.84
Ste24 endopeptidase.
based on mapping to UniProt O75844
The peptide bond hydrolyzed can be designated -C-|-A-A-X 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.
-!- One of two enzymes that can catalyze this processing step for mating a-factor in Saccharomyces cerevisiae. -!- Subsequently, the S-isoprenylated cysteine residue that forms the new C-terminus is methyl-esterified and forms a hydrophobic membrane- anchor. -!- Belongs to peptidase family M48.

UniProtKB Entries (1)

O75844
FACE1_HUMAN
Homo sapiens
CAAX prenyl protease 1 homolog

PDB Structure

PDB 4AW6
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The Structural Basis of Zmpste24-Dependent Laminopathies.
Quigley, A., Dong, Y.Y., Pike, A.C.W., Dong, L., Shrestha, L., Berridge, G., Stansfeld, P.J., Sansom, M.S.P., Edwards, A.M., Bountra, C., von Delft, F., Bullock, A.N., Burgess-Brown, N.A., Carpenter, E.P.
Science