Preflagellin peptidase

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.
Preflagellin peptidase
Identifiers
EC number3.4.23.52
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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.
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