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 15377 |
||||||||||
| PubChem |
22247451 962 22247451 962 |
||||||||||
| 1npmA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1npmB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1npmA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1npmB02 |
|
|
|
|
|
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 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1npmB01 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1npmA02 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1npmB02 |
|
|
|
|
|
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, |
| 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, |
| 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, |
| 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, |
| Created | Updated |
|---|---|
| 2011-02-16 | 2012-07-31 |