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.
PMID9224881.
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.
PMID9224881.