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Preflagellin peptidase

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Preflagellin peptidase
Identifiers
EC no.3.4.23.52
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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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.

This aspartic peptidase is present in Archaea.

References

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  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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