Preflagellin peptidase
| Preflagellin peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 with systematic name '.[1][2][3] This enzyme catalyses the following chemical reaction
- 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
- ↑ Bardy, S.L.; Jarrell, K.F. (2002). "FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity". FEMS Microbiol. Lett. 208 (1): 53–59. doi:10.1111/j.1574-6968.2002.tb11060.x. PMID 11934494.
- ↑ Ng, S.Y.; VanDyke, D.J.; Chaban, B.; Wu, J.; Nosaka, Y.; Aizawa, S.; Jarrell, K.F. (2009). "Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD". J. Bacteriol. 191: 6732–6740. doi:10.1128/JB.00673-09. PMID 19717585.
- ↑ Hu, J.; Xue, Y.; Lee, S.; Ha, Y. (2011). "The crystal structure of GXGD membrane protease FlaK". Nature. 475: 528–531. doi:10.1038/nature10218. PMID 21765428.
External links
- Preflagellin peptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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