EzCatDB: D00497
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DB codeD00497
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.3.4.21.35

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,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
UniProtKBKEGG

P00759
Protein nameTonintissue 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
SynonymsEC 3.4.21.35
Esterase 1
Glandular kallikrein-2
rGK-2
RSKG-5
S2 kallikrein
RefSeqNP_036809.1 (Protein)
NM_012677.1 (DNA/RNA sequence)
MEROPSS01.172 (Serine)
PfamPF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberP00759
Entry nameKLK2_RAT
ActivityPreferential 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.
SubunitMonomer.
Subcellular location
CofactorBinds 1 zinc ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00038C00017C00012C00769C00001C00012C01505C00306I00087I00085I00086
CompoundZincProteinPeptideKininogenH2OPeptideKallidinBradykininPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typeheavy metalpeptide/proteinpeptide/proteinpeptide/proteinH2Opeptide/proteinamino acids,amine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,imine group,lipid,peptide/proteinamino acids,amine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,imine group,lipid,peptide/protein


ChEBI29105



15377

6102
3165



PubChem32051



22247451
962

5311111
439201



                   
1tonA01UnboundUnboundUnboundUnbound UnboundUnboundUnbound   
1tonA02Bound:_ZNUnboundUnboundUnbound UnboundUnboundUnbound   

Active-site residues
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
           
1tonA01SER 195
 
GLY 193;SER 195
1tonA02HIS 57;ASP 102
HIS 57;HIS 97;HIS 99(Zinc binding)
 


references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID88011252
PubMed ID2821276
JournalJ Mol Biol
Year1987
Volume195
Pages373-96
AuthorsFujinaga M, James MN
TitleRat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution.
Related PDB1ton
Related UniProtKBP00759
[2]
PubMed ID8148470
JournalDrug Des Discov
Year1993
Volume10
Pages297-317
AuthorsBarth A, Wahab M, Brandt W, Frost K
TitleClassification of serine proteases derived from steric comparisons of their active sites.
[3]
PubMed ID9116171
JournalDrug Des Discov
Year1994
Volume12
Pages89-111
AuthorsBarth A, Frost K, Wahab M, Brandt W, Schadler HD, Franke R
TitleClassification of serine proteases derived from steric comparisons of their active sites, part II: "Ser, His, Asp arrangements in proteolytic and nonproteolytic proteins".

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.

createdupdated
2006-01-102011-02-18
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
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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