Prepilin peptidase
| Prepilin peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.23.43 | ||||||||
| CAS number | 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.[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.
References
- ↑ Lory, S.; Strom, M.S. (1997). "Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa - A review". Gene. 192: 117–121. doi:10.1016/S0378-1119(96)00830-X. PMID 9224881.
- ↑ LaPointe, C.F.; Taylor, R.K. (2000). "The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases". J. Biol. Chem. 275: 1502–1510. doi:10.1074/jbc.275.2.1502. PMID 10625704.
External links
- Prepilin peptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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