EzCatDB: M00155

DB codeM00155
RLCP classification1.13.30000.10
CATH domainDomain 12.10.70.10
Domain 22.10.25.10
Domain 32.40.20.10
Domain 42.40.10.10Catalytic domain
Domain 52.40.10.10Catalytic domain
E.C.3.4.21.68
CSA1rtf

CATH domainRelated DB codes (homologues)
2.10.25.10M00139,M00133,M00212,M00152,M00315,M00316
2.10.70.10M00139,M00315,M00316
2.40.10.10M00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411
2.40.20.10M00152,M00157

Enzyme Name
Swiss-protKEGG

P00750P98119
Protein nameTissue-type plasminogen activator (t-plasminogen activator) (t-PA) (tPA) (EC 3.4.21.68)AltName: INN=Alteplase;AltName: INN=Reteplase;Salivary plasminogen activator alpha 1t-plasminogen activator
tissue plasminogen activator
plasminogen activator, tissue-type
tissue-type plasminogen activator
tPA
t-PA
SynonymsNoneEC 3.4.21.68
DSPA alpha-1
ContainsTissue-type plasminogen activator chain A
Tissue-type plasminogen activator chain B
None


Swiss-prot:Accession NumberP00750P98119
Entry nameTPA_HUMANURT1_DESRO
ActivitySpecific cleavage of Arg-|-Val bond in plasminogen to form plasmin.Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
SubunitHeterodimer of chain A and chain B held by a disulfide bond. Binds to fibrin with high affinity. This interaction leads to an increase in the catalytic efficiency of the enzyme between 100-fold and 1000-fold, due to an increase in affinity for plasminogen. Similarly, binding to heparin increases the activation of plasminogen. Binds to annexin A2, cytokeratin-8, fibronectin and laminin. Binds to mannose receptor and the low- density lipoprotein receptor-related protein (LRP1), these proteins are involved in TPA clearance. Yet unidentified interactions on endothelial cells and vascular smooth muscle cells (VSMC) lead to a 100-fold stimulation of plasminogen activation. In addition, binding to VSMC reduces TPA inhibition by PAI-1 by 30-fold. Binds LRP1B, binding is followed by internalization and degradation.Monomer.
Subcellular locationSecreted, extracellular space.Secreted.
Cofactor



SubstratesProductsintermediates
KEGG-idC00520C00471I00087I00085I00086
CompoundPlasminogenPlasminPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinpeptide/protein


1tpgA01UnboundUnboundUnboundUnboundUnbound
1tpgA02UnboundUnboundUnboundUnboundUnbound
1tpmAUnboundUnboundUnboundUnboundUnbound
1tpnAUnboundUnboundUnboundUnboundUnbound
1pk2AUnboundUnboundUnboundUnboundUnbound
1pmlAUnboundUnboundUnboundUnboundUnbound
1pmlBUnboundUnboundUnboundUnboundUnbound
1pmlCUnboundUnboundUnboundUnboundUnbound
1tpkAUnboundUnboundUnboundUnboundUnbound
1tpkBUnboundUnboundUnboundUnboundUnbound
1tpkCUnboundUnboundUnboundUnboundUnbound
1a5hA01UnboundUnboundUnboundUnboundUnbound
1a5hB01UnboundUnboundUnboundUnboundUnbound
1a5iA01UnboundUnboundUnboundUnboundTransition-state-analogue:GLU-GLY-ARG-CH2
1bdaA01UnboundUnboundUnboundUnboundTransition-state-analogue:DSY-GLU-GLY-ARG-CH2
1bdaB01UnboundUnboundUnboundUnboundTransition-state-analogue:DSY-GLU-GLY-ARG-CH2
1rtfB01UnboundUnboundUnboundUnboundUnbound
1a5hA02UnboundUnboundUnboundUnboundUnbound
1a5hB02UnboundUnboundUnboundUnboundUnbound
1a5iA02UnboundUnboundUnboundUnboundUnbound
1bdaA02UnboundUnboundUnboundUnboundUnbound
1bdaB02UnboundUnboundUnboundUnboundUnbound
1rtfB02UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swoss-prot; P00750, P98119 & literature [21]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysiscomment
1tpgA01



1tpgA02


mutant C83S
1tpmA



1tpnA



1pk2A



1pmlA
ASN 26;LYS 33;VAL 34;TYR 35;HIS 64(Chloride binding)


1pmlB
ASN 26;LYS 33;VAL 34;TYR 35;HIS 64(Chloride binding)


1pmlC
ASN 26;LYS 33;VAL 34;TYR 35;HIS 64(Chloride binding)


1tpkA
ASN 26;LYS 33;VAL 34;TYR 35;HIS 64(Chloride binding)


1tpkB
ASN 26;LYS 33;VAL 34;TYR 35;HIS 64(Chloride binding)


1tpkC
ASN 26;LYS 33;VAL 34;TYR 35;HIS 64(Chloride binding)


1a5hA01SER 195

GLY 193;SER 195

1a5hB01SER 195

GLY 193;SER 195

1a5iA01SER 195

GLY 193;SER 195

1bdaA01SER 195

GLY 193;SER 195

1bdaB01SER 195

GLY 193;SER 195

1rtfB01SER 195

GLY 193;SER 195

1a5hA02HIS 57;ASP 102



1a5hB02HIS 57;ASP 102



1a5iA02HIS 57;ASP 102



1bdaA02HIS 57;ASP 102



1bdaB02HIS 57;ASP 102



1rtfB02HIS 57;ASP 102





references
[1]
PubMed ID6685059
JournalFEBS Lett
Year1983
Volume163
Pages37-41
AuthorsBanyai L, Varadi A, Patthy L
TitleCommon evolutionary origin of the fibrin-binding structures of fibronectin and tissue-type plasminogen activator.
[2]
PubMed ID3030730
JournalEMBO J
Year1986
Volume5
Pages3525-30
AuthorsVerheijen JH, Caspers MP, Chang GT, de Munk GA, Pouwels PH, Enger-Valk BE
TitleInvolvement of finger domain and kringle 2 domain of tissue-type plasminogen activator in fibrin binding and stimulation of activity by fibrin.
[3]
PubMed ID3021732
JournalJ Biol Chem
Year1986
Volume261
Pages14214-8
Authorsvan Zonneveld AJ, Veerman H, Pannekoek H
TitleOn the interaction of the finger and the kringle-2 domain of tissue-type plasminogen activator with fibrin. Inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid.
[4]
PubMed ID3088564
JournalProc Natl Acad Sci U S A
Year1986
Volume83
Pages4670-4
Authorsvan Zonneveld AJ, Veerman H, Pannekoek H
TitleAutonomous functions of structural domains on human tissue-type plasminogen activator.
[5]
PubMed ID2846282
JournalEMBO J
Year1988
Volume7
Pages2731-40
AuthorsGething MJ, Adler B, Boose JA, Gerard RD, Madison EL, McGookey D, Meidell RS, Roman LM, Sambrook J
TitleVariants of human tissue-type plasminogen activator that lack specific structural domains of the heavy chain.
[6]
CommentsSTRUCTURE BY NMR OF KRINGLE 2.
Medline ID90122799
PubMed ID2558718
JournalBiochemistry
Year1989
Volume28
Pages9350-60
AuthorsByeon IJ, Kelley RF, Llinas M
Title1H NMR structural characterization of a recombinant kringle 2 domain from human tissue-type plasminogen activator.
Related Swiss-protP00750
[7]
PubMed ID2497771
JournalBiochemistry
Year1989
Volume28
Pages1884-91
AuthorsCleary S, Mulkerrin MG, Kelley RF
TitlePurification and characterization of tissue plasminogen activator kringle-2 domain expressed in Escherichia coli.
[8]
PubMed ID2502177
JournalBiochemistry
Year1989
Volume28
Pages4047-54
AuthorsKelley RF, Cleary S
TitleEffect of residue 65 substitutions on thermal stability of tissue plasminogen activator kringle-2 domain.
[9]
PubMed ID2477307
JournalGene
Year1989
Volume79
Pages333-44
AuthorsStern A, Mattes R, Buckel P, Weidle UH
TitleFunctional topology of human tissue-type plasminogen activator: characterization of two deletion derivatives and of a duplication derivative.
[10]
PubMed ID2556697
JournalProtein Eng
Year1989
Volume3
Pages111-6
AuthorsMarkland W, Pollock D, Livingston DJ
TitleTissue-type plasminogen activator variants with domain duplications and rearrangements.
[11]
PubMed ID2108143
JournalJ Biol Chem
Year1990
Volume265
Pages5540-5
AuthorsAhern TJ, Morris GE, Barone KM, Horgan PG, Timony GA, Angus LB, Henson KS, Stoudemire JB, Langer-Safer PR, Larsen GR
TitleSite-directed mutagenesis in human tissue-plasminogen activator. Distinguishing sites in the amino-terminal region required for full fibrinolytic activity and rapid clearance from the circulation.
[12]
PubMed ID2108167
JournalJ Biol Chem
Year1990
Volume265
Pages5170-7
AuthorsBurck PJ, Berg DH, Warrick MW, Berg DT, Walls JD, Jaskunas SR, Crisel RM, Weigel B, Vlahos CJ, McClure DB, et al
TitleCharacterization of a modified human tissue plasminogen activator comprising a kringle-2 and a protease domain.
[13]
PubMed ID2115513
JournalJ Biol Chem
Year1990
Volume265
Pages12184-91
AuthorsCollen D, Lijnen HR, Bulens F, Vandamme AM, Tulinsky A, Nelles L
TitleBiochemical and functional characterization of human tissue-type plasminogen activator variants with mutagenized kringle domains.
[14]
PubMed ID2117612
JournalJ Biol Chem
Year1990
Volume265
Pages14606-11
AuthorsWilhelm OG, Jaskunas SR, Vlahos CJ, Bang NU
TitleFunctional properties of the recombinant kringle-2 domain of tissue plasminogen activator produced in Escherichia coli.
[15]
CommentsSTRUCTURE BY NMR OF KRINGLE 2.
Medline ID91200042
PubMed ID1901789
JournalEur J Biochem
Year1991
Volume197
Pages155-65
AuthorsByeon IJ, Kelley RF, Llinas M
TitleKringle-2 domain of the tissue-type plasminogen activator. 1H-NMR assignments and secondary structure.
Related Swiss-protP00750
[16]
PubMed ID1900516
JournalJ Biol Chem
Year1991
Volume266
Pages5191-201
AuthorsBennett WF, Paoni NF, Keyt BA, Botstein D, Jones AJ, Presta L, Wurm FM, Zoller MJ
TitleHigh resolution analysis of functional determinants on human tissue-type plasminogen activator.
[17]
CommentsDISULFIDE BONDS IN KRINGLE 2.
Medline ID91244765
PubMed ID1645336
JournalJ Biol Chem
Year1991
Volume266
Pages10070-2
AuthorsVlahos CJ, Wilhelm OG, Hassell T, Jaskunas SR, Bang NU
TitleDisulfide pairing of the recombinant kringle-2 domain of tissue plasminogen activator produced in Escherichia coli.
Related Swiss-protP00750
[18]
CommentsSTRUCTURE BY NMR OF KRINGLE 2.
Medline ID92106329
PubMed ID1762144
JournalJ Mol Biol
Year1991
Volume222
Pages1035-51
AuthorsByeon IJ, Llinas M
TitleSolution structure of the tissue-type plasminogen activator kringle 2 domain complexed to 6-aminohexanoic acid an antifibrinolytic drug.
Related PDB1pk2
Related Swiss-protP00750
[19]
PubMed ID1309292
JournalArch Biochem Biophys
Year1992
Volume292
Pages206-12
AuthorsDe Serrano VS, Sehl LC, Castellino FJ
TitleDirect identification of lysine-33 as the principal cationic center of the omega-amino acid binding site of the recombinant kringle 2 domain of tissue-type plasminogen activator.
[20]
PubMed ID1554717
JournalBiochemistry
Year1992
Volume31
Pages3326-35
AuthorsDe Serrano VS, Castellino FJ
TitleRole of tryptophan-74 of the recombinant kringle 2 domain of tissue-type plasminogen activator in its omega-amino acid binding properties.
[21]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF KRINGLE 2.
Medline ID92118803
PubMed ID1310033
JournalBiochemistry
Year1992
Volume31
Pages270-9
Authorsde Vos AM, Ultsch MH, Kelley RF, Padmanabhan K, Tulinsky A, Westbrook ML, Kossiakoff AA
TitleCrystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-A resolution.
Related PDB1tpk
Related Swiss-protP00750
[22]
PubMed ID1731899
JournalBiochemistry
Year1992
Volume31
Pages419-22
AuthorsEastman D, Wurm FM, van Reis R, Higgins DL
TitleA region of tissue plasminogen activator that affects plasminogen activation differentially with various fibrin(ogen)-related stimulators.
[23]
PubMed ID1315765
JournalJ Biol Chem
Year1992
Volume267
Pages9668-77
AuthorsBassel-Duby R, Jiang NY, Bittick T, Madison E, McGookey D, Orth K, Shohet R, Sambrook J, Gething MJ
TitleTyrosine 67 in the epidermal growth factor-like domain of tissue-type plasminogen activator is important for clearance by a specific hepatic receptor.
[24]
CommentsSTRUCTURE BY NMR OF 38-85.
Medline ID92292163
PubMed ID1602484
JournalJ Mol Biol
Year1992
Volume225
Pages821-33
AuthorsDowning AK, Driscoll PC, Harvey TS, Dudgeon TJ, Smith BO, Baron M, Campbell ID
TitleSolution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance.
Related PDB1tpm,1tpn
Related Swiss-protP00750
[25]
PubMed ID1321420
JournalProtein Eng
Year1992
Volume5
Pages93-100
AuthorsKohnert U, Rudolph R, Verheijen JH, Weening-Verhoeff EJ, Stern A, Opitz U, Martin U, Lill H, Prinz H, Lechner M, et al
TitleBiochemical properties of the kringle 2 and protease domains are maintained in the refolded t-PA deletion variant BM 06.022.
[26]
PubMed ID1287881
JournalThromb Haemost
Year1992
Volume68
Pages672-7
AuthorsYahara H, Matsumoto K, Maruyama H, Nagaoka T, Ikenaka Y, Yajima K, Fukao H, Ueshima S, Matsuo O
TitleRecombinant variants of tissue-type plasminogen activator containing amino acid substitutions in the finger domain.
[27]
PubMed ID8424682
JournalArch Biochem Biophys
Year1993
Volume300
Pages472-82
AuthorsRydzewski A, Castellino FJ
TitleThe effector roles of kringle 1 and kringle 2 in the enzymatic properties of recombinant tissue-type plasminogen activator as revealed by generation of recombinant molecules containing each kringle linked to the protease domain.
[28]
PubMed ID8385482
JournalBiochemistry
Year1993
Volume32
Pages3540-8
AuthorsDe Serrano VS, Castellino FJ
TitleSpecific anionic residues of the recombinant kringle 2 domain of tissue-type plasminogen activator that are responsible for stabilization of its interaction with omega-amino acid ligands.
[29]
PubMed ID8449917
JournalJ Biol Chem
Year1993
Volume268
Pages5550-6
AuthorsLubin IM, Caban R, Runge MS
TitleThe tissue plasminogen activator finger domain confers fibrin-dependent enhancement of catalytic activity to single-chain urokinase-type plasminogen activator.
[30]
PubMed ID8030371
JournalActa Biochim Pol
Year1994
Volume41
Pages25-34
AuthorsPietrucha T, Stec WJ, Okruszek A, Uznanski B, Koziolkiewicz M, Wilk A, Plucienniczak A, Swiatkowska M, Cierniewski CS
TitleThe epidermal growth factor-like domain from tissue plasminogen activator. Cloning in E. coli, purification and ESR studies of its interaction with human blood platelets.
[31]
PubMed ID8142348
JournalBiochemistry
Year1994
Volume33
Pages3509-14
AuthorsDe Serrano VS, Castellino FJ
TitleInvolvement of tyrosine-76 of the kringle 2 domain of tissue-type plasminogen activator in its thermal stability and its omega-amino acid ligand binding site.
[32]
PubMed ID8312251
JournalBiochemistry
Year1994
Volume33
Pages1340-4
AuthorsDe Serrano VS, Castellino FJ
TitleRole of the strictly conserved tryptophan-25 residue in the stabilization of the structure and in the ligand binding properties of the kringle 2 domain of tissue-type plasminogen activator.
[33]
PubMed ID8175674
JournalJ Biol Chem
Year1994
Volume269
Pages12639-44
AuthorsHorrevoets AJ, Smilde A, de Vries C, Pannekoek H
TitleThe specific roles of finger and kringle 2 domains of tissue-type plasminogen activator during in vitro fibrinolysis.
[34]
CommentsX-ray crystallography
PubMed ID8069221
JournalProtein Sci
Year1994
Volume3
Pages898-910
AuthorsPadmanabhan K, Wu TP, Ravichandran KG, Tulinsky A
TitleKringle-kringle interactions in multimer kringle structures.
Related PDB1pmk,1pml
[35]
PubMed ID7740461
JournalThromb Haemost
Year1994
Volume72
Pages900-5
AuthorsStringer HA, van Swieten P, Horrevoets AJ, Smilde A, Pannekoek H
TitleThe role of the finger domain of tissue-type plasminogen activator (t-PA) and plasminogen activator inhibitor 1 (PAI-1) in initiation and progression of thrombolysis.
[36]
PubMed ID7893685
JournalBiochemistry
Year1995
Volume34
Pages2739-50
AuthorsByeon IJ, Kelley RF, Mulkerrin MG, An SS, Llinas M
TitleLigand binding to the tissue-type plasminogen activator kringle 2 domain: structural characterization by 1H-NMR.
[37]
PubMed ID7711052
JournalBiochim Biophys Acta
Year1995
Volume1248
Pages1-10
AuthorsRudd PM, Woods RJ, Wormald MR, Opdenakker G, Downing AK, Campbell ID, Dwek RA
TitleThe effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator.
[38]
PubMed ID8530479
JournalJ Biol Chem
Year1995
Volume270
Pages30486-90
AuthorsSmith JW, Tachias K, Madison EL
TitleProtein loop grafting to construct a variant of tissue-type plasminogen activator that binds platelet integrin alpha IIb beta 3.
[39]
PubMed ID7479691
JournalProtein Eng
Year1995
Volume8
Pages293-300
AuthorsBakker AH, Rehberg EF, Marotti KR, Verheijen JH
TitleThe position of the structurally autonomous kringle 2 domain influences the functional features of tissue-type plasminogen activator.
[40]
CommentsSTRUCTURE BY NMR OF 36-126.
Medline ID96027104
PubMed ID7582899
JournalStructure
Year1995
Volume3
Pages823-33
AuthorsSmith BO, Downing AK, Driscoll PC, Dudgeon TJ, Campbell ID
TitleThe solution structure and backbone dynamics of the fibronectin type I and epidermal growth factor-like pair of modules of tissue-type plasminogen activator.
Related PDB1tpg
Related Swiss-protP00750
[41]
PubMed ID8605163
JournalBiochemistry
Year1996
Volume35
Pages3270-6
AuthorsHu CK, Kohnert U, Sturzebecher J, Fischer S, Llinas M
TitleComplexation of the tissue plasminogen activator protease with benzamidine-type inhibitors: interference by the kringle 2 module.
[42]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CATALYTIC DOMAIN.
Medline ID96200985
PubMed ID8613982
JournalJ Mol Biol
Year1996
Volume258
Pages117-35
AuthorsLamba D, Bauer M, Huber R, Fischer S, Rudolph R, Kohnert U, Bode W
TitleThe 2.3 A crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator.
Related PDB1rtf
Related Swiss-protP00750
[43]
PubMed ID8736495
JournalProtein Eng
Year1996
Volume9
Pages283-90
AuthorsSehl LC, Nguyen HV, Berleau LT, Arcila P, Bennett WF, Keyt BA
TitleLocating the unpaired cysteine of tissue-type plasminogen activator.
[44]
PubMed ID9201906
JournalBiochemistry
Year1997
Volume36
Pages7652-63
AuthorsChang Y, Zajicek J, Castellino FJ
TitleRole of tryptophan-63 of the kringle 2 domain of tissue-type plasminogen activator in its thermal stability, folding, and ligand binding properties.
[45]
CommentsTISSUE=Salivary gland;
Medline ID98022741
PubMed ID9354616
JournalBiochemistry
Year1997
Volume36
Pages13483-93
AuthorsRenatus M, Stubbs MT, Huber R, Bringmann P, Donner P, Schleuning WD, Bode W
TitleCatalytic domain structure of vampire bat plasminogen activator: a molecular paradigm for proteolysis without activation cleavage.
Related PDB1a5i
Related Swiss-protP98119
[46]
PubMed ID9434908
JournalCurr Opin Struct Biol
Year1997
Volume7
Pages865-72
AuthorsBode W, Renatus M
TitleTissue-type plasminogen activator: variants and crystal/solution structures demarcate structural determinants of function.
[47]
CommentsX-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF CATALYTIC DOMAIN.
Medline ID97449126
PubMed ID9305622
JournalEMBO J
Year1997
Volume16
Pages4797-805
AuthorsRenatus M, Engh RA, Stubbs MT, Huber R, Fischer S, Kohnert U, Bode W
TitleLysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA.
Related PDB1bda
Related Swiss-protP00750
[48]
CommentsX-ray crystallography
PubMed ID9268299
JournalJ Biol Chem
Year1997
Volume272
Pages21713-9
AuthorsRenatus M, Bode W, Huber R, Sturzebecher J, Prasa D, Fischer S, Kohnert U, Stubbs MT
TitleStructural mapping of the active site specificity determinants of human tissue-type plasminogen activator. Implications for the design of low molecular weight substrates and inhibitors.
Related PDB1a5h
[49]
PubMed ID10543954
JournalJ Mol Biol
Year1999
Volume293
Pages613-27
AuthorsDekker RJ, Eichinger A, Stoop AA, Bode W, Pannekoek H, Horrevoets AJ
TitleThe variable region-1 from tissue-type plasminogen activator confers specificity for plasminogen activator inhibitor-1 to thrombin by facilitating catalysis: release of a kinetic block by a heterologous protein surface loop.
[50]
PubMed ID10408340
JournalJ Pept Res
Year1999
Volume53
Pages656-64
AuthorsChang Y, Nilsen SL, Castellino FJ
TitleFunctional and structural consequences of aromatic residue substitutions within the kringle-2 domain of tissue-type plasminogen activator.
[51]
PubMed ID10744692
JournalJ Biol Chem
Year2000
Volume275
Pages10112-20
AuthorsStewart RJ, Fredenburgh JC, Leslie BA, Keyt BA, Rischke JA, Weitz JI
TitleIdentification of the mechanism responsible for the increased fibrin specificity of TNK-tissue plasminogen activator relative to tissue plasminogen activator.
[52]
PubMed ID12696753
JournalCurr Top Dev Biol
Year2003
Volume54
Pages263-312
AuthorsEllis V
TitlePlasminogen activation at the cell surface.
[53]
PubMed ID14500731
JournalJ Biol Chem
Year2003
Volume278
Pages48197-203
AuthorsPerron MJ, Blouse GE, Shore JD
TitleDistortion of the catalytic domain of tissue-type plasminogen activator by plasminogen activator inhibitor-1 coincides with the formation of stable serpin-proteinase complexes.

comments
This enzyme belongs to the peptidase family-S1.
This enzyme is composed of six domains; fibronectin type-I domain, EGF-like domain, Kringle1 domain, Kringle2 domain and catalytic domains of serine protease.
The PDB structures correspond to the following domains.
(PDB;1tpg, Swiss-prot;P00750, residues 36-126 [EGF-like/Kringle1 domain],
PDB;1pk2, Swiss-prot;P00750, residues 209-297 [klingle2 domain],
PDB;1a5hA, Swiss-prot;P00750, residues 311-562 [Catalytic domain]).
As this enzyme has got a classical catalytic triad composed of Ser/His/Asp, which is the same as that of trypsin (D00197 in EzCatDB), it should have a similar mechanism.

createdupdated
2004-08-132011-02-21
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 2010)
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)

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