KEGG   ENZYME: 3.4.21.118Help
Entry
EC 3.4.21.118               Enzyme                                 

Name
kallikrein 8;
KLK8;
PRSS19;
human kallikrein 8;
hK8;
mK8;
ovasin;
tumor-associated differentially expressed gene 14;
TADG-14;
NP;
neuropsin
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
Comment
The enzyme is activated by removal of an N-terminal prepropeptide [2,4]. The highest amidolytic activity is observed using Boc-Val-Pro-Arg!7-amido-4-methylcoumarin, which is a substrate of alpha-thrombin [2,4]. Substrates lacking basic amino acids in the P1 position are not cleaved [4]. The enzyme degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen [3] and is associated with diseases such as ovarian cancer and Alzheimer's disease [4]. Belongs in peptidase family S1A.
History
EC 3.4.21.118 created 2006
Orthology
K08650  
kallikrein 8
Genes
HSA: 
11202(KLK8)
PTR: 
456239(KLK8)
GGO: 
101151682(KLK8)
PON: 
100437370(KLK8)
NLE: 
100587419(KLK8)
MCC: 
719488(KLK8)
MCF: 
102143235(KLK8)
CSAB: 
103235109(KLK8)
RRO: 
104667249(KLK8)
CJC: 
100404633(KLK8)
SBQ: 
101047321(KLK8)
MMU: 
259277(Klk8)
RNO: 
308565(Klk8)
CGE: 
100752953(Klk8)
NGI: 
103743767(Klk8)
HGL: 
101715440(Klk8)
OCU: 
100344291(KLK8)
TUP: 
102468122
CFA: 
484352(KLK8)
AML: 
100476177(KLK8)
UMR: 
103657288(KLK8)
FCA: 
101090308(KLK8)
PTG: 
102964756(KLK8)
AJU: 
106989678(KLK8)
BTA: 
618438(KLK8)
BOM: 
102281911(KLK8)
PHD: 
102316246(KLK8)
CHX: 
102178849(KLK8)
OAS: 
101112755(KLK8)
CFR: 
102521031(KLK8)
ECB: 
100067301(KLK8)
MYB: 
102241466(KLK8)
MYD: 
102764579(KLK8)
HAI: 
109391034(KLK8)
PALE: 
102893463(KLK8)
LAV: 
100659511
SHR: 
100933656(KLK8)
CJO: 
107307352
AAM: 
106494189
XMA: 
102230174
SASA: 
106564436 106594015 106596927
 » show all
Taxonomy
Reference
1  [PMID:7623137]
  Authors
Chen ZL, Yoshida S, Kato K, Momota Y, Suzuki J, Tanaka T, Ito J, Nishino H, Aimoto S, Kiyama H, et al.
  Title
Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus.
  Journal
J. Neurosci. 15 (1995) 5088-97.
  Sequence
[mmu:259277]
Reference
2  [PMID:9556608]
  Authors
Shimizu C, Yoshida S, Shibata M, Kato K, Momota Y, Matsumoto K, Shiosaka T, Midorikawa R, Kamachi T, Kawabe A, Shiosaka S.
  Title
Characterization of recombinant and brain neuropsin, a plasticity-related serine protease.
  Journal
J. Biol. Chem. 273 (1998) 11189-96.
  Sequence
[mmu:259277]
Reference
3  [PMID:16337200]
  Authors
Rajapakse S, Ogiwara K, Takano N, Moriyama A, Takahashi T.
  Title
Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins.
  Journal
FEBS. Lett. 579 (2005) 6879-84.
  Sequence
[hsa:11202]
Reference
4  [PMID:16800733]
  Authors
Kishi T, Cloutier SM, Kundig C, Deperthes D, Diamandis EP.
  Title
Activation and enzymatic characterization of recombinant human kallikrein 8.
  Journal
Biol. Chem. 387 (2006) 723-31.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
171715-15-4
DBGET integrated database retrieval system