EzCatDB: D00211
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DB codeD00211
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.3.4.21.32

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,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

P00771
Protein nameBrachyurinbrachyurin
Uca pugilator collagenolytic proteinase
crab protease I
crab protease II
SynonymsEC 3.4.21.32
Collagenolytic protease
MEROPSS01.122 (Serine)
PfamPF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberP00771
Entry nameCOGS_UCAPU
ActivityHydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00012C00211C00001C00017C00012I00087I00085I00086
CompoundProteinPeptideCollagenH2OProteinPeptidePeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinpeptide/proteinamine group,carboxyl group,peptide/proteinH2Opeptide/proteinpeptide/protein


ChEBI


15377





PubChem


962
22247451





                 
1azzA01Analogue:MET 84-MET 85(chain C)UnboundUnbound UnboundUnbound   
1azzB01Analogue:MET 84-MET 85(chain D)UnboundUnbound UnboundUnbound   
1azzA02UnboundUnboundUnbound UnboundUnbound   
1azzB02UnboundUnboundUnbound UnboundUnbound   

Active-site residues
resource
Swiss-prot;P00771 & literature [8], [12], [14], [16]
pdbCatalytic residuesMain-chain involved in catalysis
          
1azzA01SER 195
GLY 193;SER 195
1azzB01SER 195
GLY 193;SER 195
1azzA02HIS 57;ASP 102
 
1azzB02HIS 57;ASP 102
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[14]Fig.1

references
[1]
PubMed ID6781531
JournalBiochemistry
Year1980
Volume19
Pages6089-95
AuthorsGrant GA, Eisen AZ
TitleSubstrate specificity of the collagenolytic serine protease from Uca pugilator: studies with noncollagenous substrates.
[2]
PubMed ID6756469
JournalBiochemistry
Year1982
Volume21
Pages5183-9
AuthorsWelgus HG, Grant GA, Jeffrey JJ, Eisen AZ
TitleSubstrate specificity of the collagenolytic serine protease from Uca pugilator: studies with collagenous substrates.
[3]
PubMed ID6337626
JournalBiochemistry
Year1983
Volume22
Pages354-8
AuthorsGrant GA, Sacchettini JC, Welgus HG
TitleA collagenolytic serine protease with trypsin-like specificity from the fiddler crab Uca pugilator.
[4]
PubMed ID6305411
JournalBiochemistry
Year1983
Volume22
Pages2228-33
AuthorsWelgus HG, Grant GA
TitleDegradation of collagen substrates by a trypsin-like serine protease from the fiddler crab Uca pugilator.
[5]
Medline ID94208517
PubMed ID8156987
JournalEMBO J
Year1994
Volume13
Pages1502-7
AuthorsMcGrath ME, Erpel T, Bystroff C, Fletterick RJ
TitleMacromolecular chelation as an improved mechanism of protease inhibition: structure of the ecotin-trypsin complex.
[6]
PubMed ID8034725
JournalJ Biol Chem
Year1994
Volume269
Pages19565-72
AuthorsTsu CA, Perona JJ, Schellenberger V, Turck CW, Craik CS
TitleThe substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen cleavage sites.
[7]
Medline ID95276656
PubMed ID7757004
JournalProtein Sci
Year1995
Volume4
Pages141-8
AuthorsMcGrath ME, Gillmor SA, Fletterick RJ
TitleEcotin: lessons on survival in a protease-filled world.
[8]
PubMed ID7795518
JournalProtein Sci
Year1995
Volume4
Pages337-60
AuthorsPerona JJ, Craik CS
TitleStructural basis of substrate specificity in the serine proteases.
[9]
PubMed ID7788296
JournalStructure
Year1995
Volume3
Pages309-16
AuthorsSchiltz M, Fourme R, Broutin I, Prange T
TitleThe catalytic site of serine proteinases as a specific binding cavity for xenon.
[10]
PubMed ID8626718
JournalJ Biol Chem
Year1996
Volume271
Pages11563-70
AuthorsTsu CA, Craik CS
TitleSubstrate recognition by recombinant serine collagenase 1 from Uca pugilator.
[11]
Medline ID97084808
PubMed ID8931142
JournalProtein Sci
Year1996
Volume5
Pages2236-47
AuthorsShin DH, Song HK, Seong IS, Lee CS, Chung CH, Suh SW
TitleCrystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND REVISIONS
Medline ID97299771
PubMed ID9154920
JournalBiochemistry
Year1997
Volume36
Pages5381-92
AuthorsPerona JJ, Tsu CA, Craik CS, Fletterick RJ
TitleCrystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix.
Related PDB1azz
Related UniProtKBP00771
[13]
PubMed ID9154921
JournalBiochemistry
Year1997
Volume36
Pages5393-401
AuthorsTsu CA, Perona JJ, Fletterick RJ, Craik CS
TitleStructural basis for the broad substrate specificity of fiddler crab collagenolytic serine protease 1.
[14]
PubMed ID9374470
JournalJ Biol Chem
Year1997
Volume272
Pages29987-90
AuthorsPerona JJ, Craik CS
TitleEvolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold.
[15]
PubMed ID11121112
JournalEur J Biochem
Year2001
Volume268
Pages127-31
AuthorsBenjamin DC, Kristjansdottir S, Gudmundsdottir A
TitleIncreasing the thermal stability of euphauserase. A cold-active and multifunctional serine protease from Antarctic krill.
[16]
PubMed ID12437096
JournalBiol Chem
Year2002
Volume383
Pages1125-31
AuthorsGudmundsdottir A
TitleCold-adapted and mesophilic brachyurins.
[17]
PubMed ID14731305
JournalBMC Struct Biol
Year2004
Volume4
Pages2
AuthorsRudenskaya GN, Kislitsin YA, Rebrikov DV
TitleCollagenolytic serine protease PC and trypsin PC from king crab Paralithodes camtschaticus: cDNA cloning and primary structure of the enzymes.
[18]
PubMed ID15014068
JournalJ Biol Chem
Year2004
Volume279
Pages21500-10
AuthorsWlodawer A, Li M, Gustchina A, Tsuruoka N, Ashida M, Minakata H, Oyama H, Oda K, Nishino T, Nakayama T
TitleCrystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity.

comments
This enzyme belongs to the peptidase family-S1.
As this enzyme has got a catalytic triad composed of Ser/His/Asp, it should have a similar mechanism to that of trypsin (D00197 in EzCatDB).

createdupdated
2004-04-272011-02-18
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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