Enzyme responsible for maturing type 4 pilins
Prepilin peptidase |
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Identifiers |
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EC no. | 3.4.23.43 |
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CAS no. | 202833-59-8 |
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Databases |
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IntEnz | IntEnz view |
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BRENDA | BRENDA entry |
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ExPASy | NiceZyme view |
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KEGG | KEGG entry |
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MetaCyc | metabolic pathway |
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PRIAM | profile |
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PDB structures | RCSB PDB PDBe PDBsum |
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Search |
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PMC | articles |
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PubMed | articles |
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NCBI | proteins |
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Type IV leader peptidase family (A24) |
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Identifiers |
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Symbol | Peptidase_A24 |
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Pfam | PF01478 |
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InterPro | IPR000045 |
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Available protein structures: |
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Pfam | structures / ECOD |
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PDB | RCSB PDB; PDBe; PDBj |
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PDBsum | structure summary |
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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
- ^ 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.
- ^ 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.
External links
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