Preflagellin peptidase
| Preflagellin peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.52 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Preflagellin peptidase (EC 3.4.23.52, FlaK) is an enzyme that catalyses the following chemical reaction:[1][2][3]
- Cleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly- or Lys-Gly-, to release flagellin.
This aspartic peptidase is present in Archaea.
References
[edit]- ^ Bardy SL, Jarrell KF (February 2002). "FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity". FEMS Microbiology Letters. 208 (1): 53–9. doi:10.1111/j.1574-6968.2002.tb11060.x. PMID 11934494.
- ^ Ng SY, VanDyke DJ, Chaban B, Wu J, Nosaka Y, Aizawa S, Jarrell KF (November 2009). "Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD". Journal of Bacteriology. 191 (21): 6732–40. doi:10.1128/JB.00673-09. PMC 2795283. PMID 19717585.
- ^ Hu J, Xue Y, Lee S, Ha Y (July 2011). "The crystal structure of GXGD membrane protease FlaK". Nature. 475 (7357): 528–31. doi:10.1038/nature10218. PMC 3894692. PMID 21765428.
External links
[edit]- Preflagellin+peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
