Prepilin peptidase explained

Prepilin peptidase
Ec Number:	3.4.23.43
Cas Number:	202833-59-8

Prepilin peptidase 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.

External links

• • MEROPS A24

Notes and References

1. Lory S, Strom MS . Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa--a review . Gene . 192 . 1 . 117–21 . June 1997 . 9224881 . 10.1016/S0378-1119(96)00830-X .
2. LaPointe CF, Taylor RK . The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases . The Journal of Biological Chemistry . 275 . 2 . 1502–10 . January 2000 . 10625704 . 10.1074/jbc.275.2.1502 . free .