DB code: D00497

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. 3.4.21.35
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 M00217 M00216 D00528 D00848 D00850 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
P00759 Tonin
EC 3.4.21.35
Esterase 1
Glandular kallikrein-2
rGK-2
RSKG-5
S2 kallikrein
NP_036809.1 (Protein)
NM_012677.1 (DNA/RNA sequence)
S01.172 (Serine)
PF00089 (Trypsin)
[Graphical View]

KEGG enzyme name
tissue kallikrein
glandular kallikrein
pancreatic kallikrein
submandibular kallikrein
submaxillary kallikrein
kidney kallikrein
urinary kallikrein
kallikrein
salivary kallikrein
kininogenin
kininogenase
callicrein
glumorin
padreatin
padutin
kallidinogenase
bradykininogenase
depot-padutin
urokallikrein
dilminal D
onokrein P

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00759 KLK2_RAT Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa. Monomer. Binds 1 zinc ion per subunit.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C00017 C00012 C00769 C00001 C00012 C01505 C00306 I00087 I00085 I00086
E.C.
Compound Zinc Protein Peptide Kininogen H2O Peptide Kallidin Bradykinin Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type heavy metal peptide/protein peptide/protein peptide/protein H2O peptide/protein amino acids,amine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,imine group,lipid,peptide/protein amino acids,amine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,imine group,lipid,peptide/protein
ChEBI 29105
15377
6102
3165
PubChem 32051
22247451
962
5311111
439201
1tonA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tonA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1tonA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1tonA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102 HIS 57;HIS 97;HIS 99(Zinc binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID 88011252
PubMed ID 2821276
Journal J Mol Biol
Year 1987
Volume 195
Pages 373-96
Authors Fujinaga M, James MN
Title Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution.
Related PDB 1ton
Related UniProtKB P00759
[2]
Resource
Comments
Medline ID
PubMed ID 8148470
Journal Drug Des Discov
Year 1993
Volume 10
Pages 297-317
Authors Barth A, Wahab M, Brandt W, Frost K
Title Classification of serine proteases derived from steric comparisons of their active sites.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9116171
Journal Drug Des Discov
Year 1994
Volume 12
Pages 89-111
Authors Barth A, Frost K, Wahab M, Brandt W, Schadler HD, Franke R
Title Classification of serine proteases derived from steric comparisons of their active sites, part II: "Ser, His, Asp arrangements in proteolytic and nonproteolytic proteins".
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the peptidase family-S1.
This enzyme has got a catalytic triad composed of Ser195/His57/Asp102, similar to that of trypsin (D00197 in EzCatDB). However, His57 orients differently from other homologous peptidases, forming a binding site for zinc ion, along with His97 and His99. Thus, the zinc ion seems to play an inhibitory role, instead of a cofactor.

Created Updated
2006-01-10 2011-02-18