DB code: D00850

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
E.C. 3.4.21.118
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.40.10.10 : Thrombin, subunit H M00139 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq MEROPS Pfam
Q61955 Kallikrein-8
mK8
EC 3.4.21.118
Neuropsin
NP
Serine protease 19
NP_032966.1 (Protein)
NM_008940.2 (DNA/RNA sequence)
S01.244 (Serine)
PF00089 (Trypsin)
[Graphical View]

KEGG enzyme name
Kallikrein 8
KLK8
PRSS19
Human kallikrein 8
hK8
mK8
Ovasin
Tumor-associated differentially expressed gene 14
TADG-14
NP
Neuropsin

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q61955 NRPN_MOUSE Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys. Interacts with SPINK9 (By similarity). Secreted. Cytoplasm. Note: Shows a cytoplasmic distribution in the keratinocytes.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00012 C00001 C00012 I00087 I00085 I00086
E.C.
Compound Peptide H2O Peptide Peptidyl-Ser-tetrahedral-intermediate (with previous peptide) Acyl-enzyme(Peptidyl-Ser-acyl group) Peptidyl-Ser-tetrahedral-intermediate
Type peptide/protein H2O peptide/protein
ChEBI 15377
PubChem 22247451
962
1npmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1npmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1npmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1npmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Literature [2] & Swiss-prot;Q61955

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1npmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1npmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1npmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1npmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Figure 5, p.4505-4508

References
[1]
Resource
Comments PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
Medline ID
PubMed ID 9556608
Journal J Biol Chem
Year 1998
Volume 273
Pages 11189-96
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.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-257.
Medline ID
PubMed ID 9933620
Journal J Biol Chem
Year 1999
Volume 274
Pages 4220-4
Authors Kishi T, Kato M, Shimizu T, Kato K, Matsumoto K, Yoshida S, Shiosaka S, Hakoshima T
Title Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis.
Related PDB 1npm
Related UniProtKB Q61955
[3]
Resource
Comments
Medline ID
PubMed ID 12475199
Journal Chem Rev
Year 2002
Volume 102
Pages 4501-24
Authors Hedstrom L
Title Serine protease mechanism and specificity.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 16337200
Journal FEBS Lett
Year 2005
Volume 579
Pages 6879-84
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.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 20940292
Journal J Biol Chem
Year 2011
Volume 286
Pages 687-706
Authors Eissa A, Amodeo V, Smith CR, Diamandis EP
Title Kallikrein-related peptidase-8 (KLK8) is an active serine protease in human epidermis and sweat and is involved in a skin barrier proteolytic cascade.
Related PDB
Related UniProtKB

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.

Created Updated
2011-02-16 2012-07-31