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Prepilin peptidase

From Wikipedia, the free encyclopedia
Prepilin peptidase
Identifiers
EC no.3.4.23.43
CAS no.202833-59-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
Type IV leader peptidase family (A24)
Identifiers
SymbolPeptidase_A24
PfamPF01478
InterProIPR000045
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

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  1. ^ 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.
  2. ^ 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.
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