EzCatDB: D00850
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DB codeD00850
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 12.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 22.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.118

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00848,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
UniProtKBKEGG

Q61955
Protein nameKallikrein-8Kallikrein 8
KLK8
PRSS19
Human kallikrein 8
hK8
mK8
Ovasin
Tumor-associated differentially expressed gene 14
TADG-14
NP
Neuropsin
SynonymsmK8
EC 3.4.21.118
Neuropsin
NP
Serine protease 19
RefSeqNP_032966.1 (Protein)
NM_008940.2 (DNA/RNA sequence)
MEROPSS01.244 (Serine)
PfamPF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberQ61955
Entry nameNRPN_MOUSE
ActivityCleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys.
SubunitInteracts with SPINK9 (By similarity).
Subcellular locationSecreted. Cytoplasm. Note: Shows a cytoplasmic distribution in the keratinocytes.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00012C00001C00012I00087I00085I00086
CompoundPeptideH2OPeptidePeptidyl-Ser-tetrahedral-intermediate (with previous peptide)Acyl-enzyme(Peptidyl-Ser-acyl group)Peptidyl-Ser-tetrahedral-intermediate
Typepeptide/proteinH2Opeptide/protein


ChEBI
15377




PubChem
962
22247451




              
1npmA01Unbound UnboundUnboundUnboundUnbound
1npmB01Unbound UnboundUnboundUnboundUnbound
1npmA02Unbound UnboundUnboundUnboundUnbound
1npmB02Unbound UnboundUnboundUnboundUnbound

Active-site residues
resource
Literature [2] & Swiss-prot;Q61955
pdbCatalytic residuesMain-chain involved in catalysis
          
1npmA01SER 195
GLY 193;SER 195
1npmB01SER 195
GLY 193;SER 195
1npmA02HIS 57;ASP 102
 
1npmB02HIS 57;ASP 102
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Figure 5, p.4505-4508

references
[1]
CommentsPROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
PubMed ID9556608
JournalJ Biol Chem
Year1998
Volume273
Pages11189-96
AuthorsShimizu C, Yoshida S, Shibata M, Kato K, Momota Y, Matsumoto K, Shiosaka T, Midorikawa R, Kamachi T, Kawabe A, Shiosaka S
TitleCharacterization of recombinant and brain neuropsin, a plasticity-related serine protease.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-257.
PubMed ID9933620
JournalJ Biol Chem
Year1999
Volume274
Pages4220-4
AuthorsKishi T, Kato M, Shimizu T, Kato K, Matsumoto K, Yoshida S, Shiosaka S, Hakoshima T
TitleCrystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis.
Related PDB1npm
Related UniProtKBQ61955
[3]
PubMed ID12475199
JournalChem Rev
Year2002
Volume102
Pages4501-24
AuthorsHedstrom L
TitleSerine protease mechanism and specificity.
[4]
PubMed ID16337200
JournalFEBS Lett
Year2005
Volume579
Pages6879-84
AuthorsRajapakse S, Ogiwara K, Takano N, Moriyama A, Takahashi T
TitleBiochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins.
[5]
PubMed ID20940292
JournalJ Biol Chem
Year2011
Volume286
Pages687-706
AuthorsEissa A, Amodeo V, Smith CR, Diamandis EP
TitleKallikrein-related peptidase-8 (KLK8) is an active serine protease in human epidermis and sweat and is involved in a skin barrier proteolytic cascade.

comments
This enzyme belongs to peptidase family-S1.
Since this enzyme has got the same catalytic site as trypsin, it must catalyze the trypsin-like reaction.

createdupdated
2011-02-162012-07-31
Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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