Preflagellin peptidase explained

Preflagellin peptidase
Ec Number:	3.4.23.52

Preflagellin peptidase (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.

Notes and References

1. Bardy SL, Jarrell KF . FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity . FEMS Microbiology Letters . 208 . 1 . 53–9 . February 2002 . 11934494 . 10.1111/j.1574-6968.2002.tb11060.x . free .
2. Ng SY, VanDyke DJ, Chaban B, Wu J, Nosaka Y, Aizawa S, Jarrell KF . Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD . Journal of Bacteriology . 191 . 21 . 6732–40 . November 2009 . 19717585 . 2795283 . 10.1128/JB.00673-09 .
3. Hu J, Xue Y, Lee S, Ha Y . The crystal structure of GXGD membrane protease FlaK . Nature . 475 . 7357 . 528–31 . July 2011 . 21765428 . 3894692 . 10.1038/nature10218 .