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
Search PMC articles PubMed articles NCBI proteins

Preflagellin peptidase (EC 3.4.23.52, designated 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

1. 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.
2. 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.
3. 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

• Preflagellin+peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)