| Prepilin peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.43 | ||||||||
| CAS no. | 202833-59-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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.
This enzyme is present on the surface of many species of bacteria. All known enzymes with this activity are of the MEROPS family A24.
References
- ^ Lory S, Strom MS (June 1997). "Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa--a review". Gene. 192 (1): 117–21. doi:10.1016/S0378-1119(96)00830-X. PMID 9224881.
- ^ LaPointe CF, Taylor RK (January 2000). "The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases". The Journal of Biological Chemistry. 275 (2): 1502–10. doi:10.1074/jbc.275.2.1502. PMID 10625704.
External links
- Prepilin+peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- MEROPS A24
This page was last edited on 27 August 2023, at 17:14