Prepilin peptidase
Enzyme responsible for maturing type 4 pilins
From Wikipedia, the free encyclopedia
Prepilin peptidase (EC 3.4.23.43) is an enzyme found in Type IV filament systems responsible for the maturation of the pilin.[1][2] This enzyme catalyses the following chemical reaction
- Typically cleaves a -Gly-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
| Prepilin peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.43 | ||||||||
| CAS no. | 202833-59-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme is present on the surface of many species of bacteria. All known enzymes with this activity are of the MEROPS family A24.
