Misplaced Pages

Kallikrein 8

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
Kallikrein 8
Identifiers
EC no.3.4.21.118
CAS no.171715-15-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Kallikrein 8 (EC 3.4.21.118, KLK8, PRSS19, human kallikrein 8, hK8, mK8, ovasin, tumor-associated differentially expressed gene 14, TADG-14, NP, neuropsin) is an enzyme. This enzyme catalyses the following chemical reaction

Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys

The enzyme is activated by removal of an N-terminal prepropeptide.

References

  1. Chen ZL, Yoshida S, Kato K, Momota Y, Suzuki J, Tanaka T, Ito J, Nishino H, Aimoto S, Kiyama H (July 1995). "Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus". The Journal of Neuroscience. 15 (7 Pt 2): 5088–97. doi:10.1523/JNEUROSCI.15-07-05088.1995. PMC 6577896. PMID 7623137.
  2. Shimizu C, Yoshida S, Shibata M, Kato K, Momota Y, Matsumoto K, Shiosaka T, Midorikawa R, Kamachi T, Kawabe A, Shiosaka S (May 1998). "Characterization of recombinant and brain neuropsin, a plasticity-related serine protease". The Journal of Biological Chemistry. 273 (18): 11189–96. doi:10.1074/jbc.273.18.11189. PMID 9556608.
  3. Rajapakse S, Ogiwara K, Takano N, Moriyama A, Takahashi T (December 2005). "Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins". FEBS Letters. 579 (30): 6879–84. doi:10.1016/j.febslet.2005.11.039. hdl:2115/985. PMID 16337200.
  4. Kishi T, Cloutier SM, Kündig C, Deperthes D, Diamandis EP (June 2006). "Activation and enzymatic characterization of recombinant human kallikrein 8" (PDF). Biological Chemistry. 387 (6): 723–31. doi:10.1515/BC.2006.091. PMID 16800733.

External links

Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes
Coagulation
Complement system
Other immune system
Venombin
Other
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal: Category: