KEGG   ENZYME: 3.4.21.118
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
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
HSA11202(KLK8)
PTR456239(KLK8)
PPS100970185(KLK8)
PON100437370(KLK8)
NLE100587419(KLK8)
HMH116478139(KLK8)
MCC719488(KLK8)
MCF102143235(KLK8)
MTHB126943165
MNI105497131(KLK8)
CSAB103235109(KLK8)
CATY105595348(KLK8)
PANU101008136(KLK8)
TGE112612813(KLK8)
MLEU105528931(KLK8)
RRO104667249(KLK8)
RBB108532406(KLK8)
TFN117064577 117091658(KLK8)
PTEH111520135(KLK8)
CANG105514719(KLK8)
CJC100404633(KLK8)
SBQ101047321(KLK8)
CIMI108291977(KLK8)
CSYR103274732(KLK8)
MMUR105865553(KLK8)
LCAT123623762(KLK8)
PCOQ105809350(KLK8)
OGA105888334(KLK8)
MMU259277(Klk8)
MCAL110297556(Klk8)
MPAH110320329(Klk8)
RNO308565(Klk8)
MCOC116102105(Klk8)
ANU117711196(Klk8)
MUN110553717(Klk8)
CGE100752953
MAUA101839688(Klk8)
PROB127213894(Klk8)
PLEU114683940(Klk8)
MORG121448412
MFOT126488150
NGI103743767(Klk8)
HGL101715440(Klk8)
CPOC100716239
CCAN109683871(Klk8)
DORD105994286(Klk8)
DSP122125632(Klk8)
PLOP125368109
NCAR124967154
MMMA107151203(Klk8)
OPI101523645(KLK8)
TUP102468122
GVR103597721(KLK8)
CFA484352(KLK8)
CLUD112645077(KLK8)
VVP112931314(KLK8)
VLG121484998
NPO129500971(KLK8)
AML100476177(KLK8)
UMR103657288(KLK8)
UAH113247321(KLK8)
UAR123778002(KLK8)
ELK111160641
LLV125089997
MPUF101689273(KLK8)
MLK131817585(KLK8)
NVS122911770
ORO101383132
EJU114199519(KLK8)
ZCA113936323(KLK8)
MLX117997972(KLK8)
NSU110572720(KLK8)
LWW102727224
FCA101090308(KLK8)
PYU121018991(KLK8)
PCOO112851203
PBG122493798(KLK8)
PVIV125153162(KLK8)
LRUF124510865
PTG102964756(KLK8)
PPAD109252984 109252986(KLK8)
PUC125915719
AJU106989678
HHV120244404(KLK8)
BTA618438(KLK8)
BOM102281911(KLK8)
BIU109571931(KLK8)
BBUB102402053(KLK8)
BBIS104995699
CHX102178849(KLK8)
OAS101112755(KLK8)
BTAX128063379(KLK8)
ODA120872028(KLK8)
CCAD122421606(KLK8)
MBEZ129546485(KLK8)
SSC110261027(KLK8)
CFR102521031
CBAI105062681(KLK8)
CDK105100154
VPC102529503(KLK8)
BMUS118885405
ECB100067301(KLK8)
EPZ103567751(KLK8)
EAI106847546(KLK8)
MYB102241466(KLK8)
MYD102764579(KLK8)
MMYO118649163(KLK8)
PKL118714912(KLK8)
EFUS103297597(KLK8)
MNA107531775(KLK8)
DRO112310176
AJM119052030
PDIC114510587
PHAS123830316
MMF118638351(KLK8)
PPAM129082708(KLK8)
HAI109391034(KLK8)
RFQ117035627(KLK8)
PALE102893463
PGIG120584034(KLK8)
PVP105307411
RAY107500461(KLK8)
TOD119249655
SARA101554967(KLK8)
LAV100659511
TMU101340570
ETF101640603
DNM101438195
MDO103092918(KLK8)
GAS123240781(KLK8)
SHR100933656(KLK8)
AFZ127556450
PCW110220141(KLK8)
OAA114811990 114812093(KLK8)
CJO107307352
NMEL110391482
OMA130262827
PCRI104025168
PADL103925967
AFOR103905999
BREG104631035
FGA104078072
NNT104403169
SHAB115603372 115603373
ACAR104531576
CVF104282761
RTD128901569
AROW112962207
NCC104941648
MSAM119898609 119898610
ONL109199930 109199932 109202569 109202581
OAU116329159 120440772
XMA102227215 102230174
XCO114140853
PRET103473950
PLAI106962246
AOCE111577596
LCF108889075
SDU111230926
SLAL111671872
SASA106564436 106594015 106596927
OMY110494920 118940083
OKE118376301
ARUT117964822
CIN100177494
FAS105266625
AGB108909605
PGW126372249
PSOJPHYSODRAFT_393864
 » show all
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 15:5088-97 (1995)
DOI:10.1523/JNEUROSCI.15-07-05088.1995
  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 273:11189-96 (1998)
DOI:10.1074/jbc.273.18.11189
  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 579:6879-84 (2005)
DOI:10.1016/j.febslet.2005.11.039
  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 387:723-31 (2006)
DOI:10.1515/BC.2006.091
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.118
IUBMB Enzyme Nomenclature: 3.4.21.118
ExPASy - ENZYME nomenclature database: 3.4.21.118
BRENDA, the Enzyme Database: 3.4.21.118
CAS: 171715-15-4

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