EzCatDB: D00432
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DB codeD00432
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.3.4.21.71

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
UniProtKBKEGG

P08419Q29461
Protein nameElastase-2AElastase-2Apancreatic elastase II
pancreatic elastase 2
SynonymsEC 3.4.21.71
Elastase-2
EC 3.4.21.71
Elastase-2
Elastase II
RefSeqNP_999274.1 (Protein)
NM_214109.1 (DNA/RNA sequence)
NP_777139.1 (Protein)
NM_174714.2 (DNA/RNA sequence)
MEROPSS01.155 (Serine)
S01.155 (Serine)
PfamPF00089 (Trypsin)
[Graphical view]
PF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberP08419Q29461
Entry nameELA2A_PIGELA2A_BOVIN
ActivityPreferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.
Subunit

Subcellular locationSecreted.Secreted.
Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00373C00001C00012I00087I00085I00086
CompoundElastinH2OPeptidePeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinH2Opeptide/protein


ChEBI
15377




PubChem439221
962
22247451




              
1bruP01Unbound UnboundUnboundIntermediate-analogue:1NBUnbound
1bruP02Unbound UnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P08419
pdbCatalytic residuesMain-chain involved in catalysis
          
1bruP01SER 195
GLY 193;SER 195
1bruP02HIS 57;ASP 102
 


references
[1]
PubMed ID6094548
JournalJ Biol Chem
Year1984
Volume259
Pages14271-8
AuthorsSwift GH, Craik CS, Stary SJ, Quinto C, Lahaie RG, Rutter WJ, MacDonald RJ
TitleStructure of the two related elastase genes expressed in the rat pancreas.
[2]
PubMed ID3635654
JournalJ Theor Biol
Year1986
Volume119
Pages107-24
AuthorsCarlson GM, MacDonald RJ, Meyer EF Jr
TitleComputer aided prediction and evaluation of the tertiary structure for rat elastase II.
[3]
PubMed ID3634756
JournalInt J Pept Protein Res
Year1986
Volume27
Pages183-90
AuthorsVered M, Gertler A, Burstein Y
TitlePartial amino acid sequence of porcine elastase II. Active site and the activation peptide regions.
[4]
PubMed ID11838546
JournalJ Protein Chem
Year2001
Volume20
Pages577-84
AuthorsAzuma K, Banshou Y, Suzuki H
TitleBovine pancreatic elastase II cleaves Gln-Ile bond.

comments
This enzyme belongs to the peptidase family-S1.
This enzyme has got a catalytic triad, composed of Ser195/His57/Asp102, suggesting that it has a similar catalytic mechanism to that of trypsin.

createdupdated
2004-10-262011-02-21


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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