Prepilin peptidase

{{Short description|Enzyme responsible for maturing type 4 pilins}}

{{Infobox enzyme

| Name = Prepilin peptidase

| EC_number = 3.4.23.43

| CAS_number = 202833-59-8

| GO_code =

| image =

| width =

| caption =

}}

{{Infobox protein family

|Pfam=PF01478

|Symbol=Peptidase_A24

|Name=Type IV leader peptidase family (A24)

|InterPro=IPR000045

}}

Prepilin peptidase ({{EC number|3.4.23.43}}) is an enzyme found in Type IV filament systems responsible for the maturation of the pilin.{{cite journal | vauthors = Lory S, Strom MS | title = Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa--a review | journal = Gene | volume = 192 | issue = 1 | pages = 117–21 | date = June 1997 | pmid = 9224881 | doi = 10.1016/S0378-1119(96)00830-X }}{{cite journal | vauthors = LaPointe CF, Taylor RK | title = The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases | journal = The Journal of Biological Chemistry | volume = 275 | issue = 2 | pages = 1502–10 | date = January 2000 | pmid = 10625704 | doi = 10.1074/jbc.275.2.1502 | doi-access = free }} 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.