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
Search PMC articles PubMed articles NCBI proteins

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

1. Bardy, S.L. and 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.
2. Ng, S.Y., VanDyke, D.J., Chaban, B., Wu, J., Nosaka, Y., Aizawa, S. and 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.
3. Hu, J., Xue, Y., Lee, S. and 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)