DB code: D00211

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. 3.4.21.32
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 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
P00771 Brachyurin
EC 3.4.21.32
Collagenolytic protease
S01.122 (Serine)
PF00089 (Trypsin)
[Graphical View]

KEGG enzyme name
brachyurin
Uca pugilator collagenolytic proteinase
crab protease I
crab protease II

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00771 COGS_UCAPU Hydrolysis 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.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00017 C00012 C00211 C00001 C00017 C00012 I00087 I00085 I00086
E.C.
Compound Protein Peptide Collagen H2O Protein Peptide Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type peptide/protein peptide/protein amine group,carboxyl group,peptide/protein H2O peptide/protein peptide/protein
ChEBI 15377
PubChem 22247451
962
1azzA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:MET_84-MET_85 (chain C) Unbound Unbound Unbound Unbound
1azzB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:MET_84-MET_85 (chain D) Unbound Unbound Unbound Unbound
1azzA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1azzB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P00771 & literature [8], [12], [14], [16]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1azzA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1azzB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1azzA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1azzB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[14]
Fig.1

References
[1]
Resource
Comments
Medline ID
PubMed ID 6781531
Journal Biochemistry
Year 1980
Volume 19
Pages 6089-95
Authors Grant GA, Eisen AZ
Title Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with noncollagenous substrates.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 6756469
Journal Biochemistry
Year 1982
Volume 21
Pages 5183-9
Authors Welgus HG, Grant GA, Jeffrey JJ, Eisen AZ
Title Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with collagenous substrates.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 6337626
Journal Biochemistry
Year 1983
Volume 22
Pages 354-8
Authors Grant GA, Sacchettini JC, Welgus HG
Title A collagenolytic serine protease with trypsin-like specificity from the fiddler crab Uca pugilator.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 6305411
Journal Biochemistry
Year 1983
Volume 22
Pages 2228-33
Authors Welgus HG, Grant GA
Title Degradation of collagen substrates by a trypsin-like serine protease from the fiddler crab Uca pugilator.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID 94208517
PubMed ID 8156987
Journal EMBO J
Year 1994
Volume 13
Pages 1502-7
Authors McGrath ME, Erpel T, Bystroff C, Fletterick RJ
Title Macromolecular chelation as an improved mechanism of protease inhibition: structure of the ecotin-trypsin complex.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8034725
Journal J Biol Chem
Year 1994
Volume 269
Pages 19565-72
Authors Tsu CA, Perona JJ, Schellenberger V, Turck CW, Craik CS
Title The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen cleavage sites.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID 95276656
PubMed ID 7757004
Journal Protein Sci
Year 1995
Volume 4
Pages 141-8
Authors McGrath ME, Gillmor SA, Fletterick RJ
Title Ecotin: lessons on survival in a protease-filled world.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 7795518
Journal Protein Sci
Year 1995
Volume 4
Pages 337-60
Authors Perona JJ, Craik CS
Title Structural basis of substrate specificity in the serine proteases.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 7788296
Journal Structure
Year 1995
Volume 3
Pages 309-16
Authors Schiltz M, Fourme R, Broutin I, Prange T
Title The catalytic site of serine proteinases as a specific binding cavity for xenon.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8626718
Journal J Biol Chem
Year 1996
Volume 271
Pages 11563-70
Authors Tsu CA, Craik CS
Title Substrate recognition by recombinant serine collagenase 1 from Uca pugilator.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID 97084808
PubMed ID 8931142
Journal Protein Sci
Year 1996
Volume 5
Pages 2236-47
Authors Shin DH, Song HK, Seong IS, Lee CS, Chung CH, Suh SW
Title Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability.
Related PDB
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND REVISIONS
Medline ID 97299771
PubMed ID 9154920
Journal Biochemistry
Year 1997
Volume 36
Pages 5381-92
Authors Perona JJ, Tsu CA, Craik CS, Fletterick RJ
Title Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix.
Related PDB 1azz
Related UniProtKB P00771
[13]
Resource
Comments
Medline ID
PubMed ID 9154921
Journal Biochemistry
Year 1997
Volume 36
Pages 5393-401
Authors Tsu CA, Perona JJ, Fletterick RJ, Craik CS
Title Structural basis for the broad substrate specificity of fiddler crab collagenolytic serine protease 1.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9374470
Journal J Biol Chem
Year 1997
Volume 272
Pages 29987-90
Authors Perona JJ, Craik CS
Title Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11121112
Journal Eur J Biochem
Year 2001
Volume 268
Pages 127-31
Authors Benjamin DC, Kristjansdottir S, Gudmundsdottir A
Title Increasing the thermal stability of euphauserase. A cold-active and multifunctional serine protease from Antarctic krill.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 12437096
Journal Biol Chem
Year 2002
Volume 383
Pages 1125-31
Authors Gudmundsdottir A
Title Cold-adapted and mesophilic brachyurins.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 14731305
Journal BMC Struct Biol
Year 2004
Volume 4
Pages 2
Authors Rudenskaya GN, Kislitsin YA, Rebrikov DV
Title Collagenolytic serine protease PC and trypsin PC from king crab Paralithodes camtschaticus: cDNA cloning and primary structure of the enzymes.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 15014068
Journal J Biol Chem
Year 2004
Volume 279
Pages 21500-10
Authors Wlodawer A, Li M, Gustchina A, Tsuruoka N, Ashida M, Minakata H, Oyama H, Oda K, Nishino T, Nakayama T
Title Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity.
Related PDB
Related UniProtKB

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).

Created Updated
2004-04-27 2011-02-18