EzCatDB: M00157

DB codeM00157
RLCP classification1.13.30120.22
CATH domainDomain 1-.-.-.-
Domain 22.40.20.10
Domain 32.40.20.10
Domain 42.40.20.10
Domain 52.40.20.10
Domain 62.40.20.10
Domain 72.40.10.10Catalytic domain
Domain 82.40.10.10Catalytic domain
E.C.3.4.21.7
CSA1ddj,1qrz

CATH domainRelated DB codes (homologues)
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,M00155,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411
2.40.20.10M00152,M00155

Enzyme Name
Swiss-protKEGG

P00747
Protein namePlasminogenplasmin
fibrinase
fibrinolysin
actase
serum tryptase
thrombolysin
SynonymsEC 3.4.21.7
ContainsPlasmin heavy chain A
Activation peptide
Angiostatin
Plasmin heavy chain A, short form
Plasmin light chain B


Swiss-prot:Accession NumberP00747
Entry namePLMN_HUMAN
ActivityPreferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.
SubunitInteracts with AMOT and CSPG4 (also true for angiostatin).
Subcellular locationSecreted.
Cofactor


SubstratesProductsintermediates
KEGG-idC00001C00290C02873C00045C00069I00087I00085I00086
CompoundH2OFibrinPeptide(Lys-, Arg-)Amino acidAlcoholPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
TypeH2Oamine group,peptide/proteinamino acids,amine group,peptide/proteinamino acidscarbohydrate


1ki0A01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ceaA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ceaB
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cebA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cebB
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1hpjA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1hpkA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pkrA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ki0A02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b2iA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1i5kA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1i5kB
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ki0A03
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1krnA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pk4A
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pmkA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pmkB
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
2pk4A
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
5hpgA
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
5hpgB
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bmlA01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bmlB01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1buiA01
UnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:GLU-GLY-MAI(chain I)
1buiB01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ddjA01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ddjB01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ddjC01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ddjD01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l4dA01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l4zA01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qrzA01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qrzB01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qrzC01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qrzD01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1rjxB01
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bmlA02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bmlB02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1buiA02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1buiB02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ddjA02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ddjB02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ddjC02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ddjD02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l4dA02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l4zA02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qrzA02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qrzB02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qrzC02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qrzD02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1rjxB02
UnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1bml, 1bui, 1qrz & Swiss-prot;P00747
pdbCatalytic residuesModified residuescomment
1ki0A01


1ceaA


1ceaB


1cebA


1cebB


1hpjA


1hpkA


1pkrA


1ki0A02


1b2iA

mutant C181T, E182S, C188G
1i5kA

mutant C4G, E56D, L72Y
1i5kB

mutant C4G, E56D, L72Y
1ki0A03

mutant N289E
1krnA


1pk4A


1pmkA


1pmkB


2pk4A


5hpgA


5hpgB


1bmlA01       

mutant S741A
1bmlB01       

mutant S741A
1buiA01SER 195


1buiB01SER 195


1ddjA01       

mutant S741A
1ddjB01       

mutant S741A
1ddjC01       

mutant S741A
1ddjD01       

mutant S741A
1l4dA01       

mutant S741A
1l4zA01       

mutant S741A
1qrzA01SER 741

mutant V673M
1qrzB01SER 741

mutant V673M
1qrzC01SER 741

mutant V673M
1qrzD01SER 741

mutant V673M
1rjxB01SER 741

mutant K698M
1bmlA02HIS 603;ASP 646
SER 578(Phospholylated)

1bmlB02HIS 603;ASP 646
SER 578(Phospholylated)

1buiA02HIS  57;ASP 102
SER  32(Phospholylated)

1buiB02HIS  57;ASP 102
SER  32(Phospholylated)

1ddjA02HIS 603;ASP 646
SER 578(Phospholylated)

1ddjB02HIS 603;ASP 646
SER 578(Phospholylated)

1ddjC02HIS 603;ASP 646
SER 578(Phospholylated)

1ddjD02HIS 603;ASP 646
SER 578(Phospholylated)

1l4dA02HIS 603;ASP 646
SER 578(Phospholylated)

1l4zA02HIS 603;ASP 646
SER 578(Phospholylated)

1qrzA02HIS 603;ASP 646
SER 578(Phospholylated)
mutant M585Q, M788L
1qrzB02HIS 603;ASP 646
SER 578(Phospholylated)
mutant M585Q, M788L
1qrzC02HIS 603;ASP 646
SER 578(Phospholylated)
mutant M585Q, M788L
1qrzD02HIS 603;ASP 646
SER 578(Phospholylated)
mutant M585Q, M788L
1rjxB02HIS 603;ASP 646
SER 578(Phospholylated)


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[49]p.906, p.907-909

references
[1]
CommentsACTIVE SITE.
Medline ID69234739
PubMed ID4240117
JournalJ Biol Chem
Year1969
Volume244
Pages3590-7
AuthorsGroskopf WR, Summaria L, Robbins KC
TitleStudies on the active center of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue.
Related Swiss-protP00747
[2]
CommentsACTIVE SITE.
Medline ID73149248
PubMed ID4694729
JournalJ Biol Chem
Year1973
Volume248
Pages1631-3
AuthorsRobbins KC, Bernabe P, Arzadon L, Summaria L
TitleThe primary structure of human plasminogen. II. The histidine loop of human plasmin: light (B) chain active center histidine sequence.
Related Swiss-protP00747
[3]
CommentsVARIANT THROMBOPHILIA THR-620.
Medline ID83065132
PubMed ID6216475
JournalProc Natl Acad Sci U S A
Year1982
Volume79
Pages6132-6
AuthorsMiyata T, Iwanaga S, Sakata Y, Aoki N
TitlePlasminogen Tochigi: inactive plasmin resulting from replacement of alanine-600 by threonine in the active site.
Related Swiss-protP00747
[4]
PubMed ID6311534
JournalEur J Biochem
Year1983
Volume135
Pages379-91
AuthorsLlinas M, De Marco A, Hochschwender SM, Laursen RA
TitleA 1H-NMR study of isolated domains from human plasminogen. Structural homology between kringles 1 and 4.
[5]
PubMed ID2933077
JournalBiochim Biophys Acta
Year1985
Volume832
Pages215-9
AuthorsAscenzi P, Torroni A, Menegatti E, Guarneri M, Amiconi G
TitleCatalytic properties of human Lys77-plasmin. A comparative steady-state and pre-steady-state study.
[6]
PubMed ID2982407
JournalBiochim Biophys Acta
Year1985
Volume827
Pages369-80
AuthorsDe Marco A, Laursen RA, Llinas M
TitleProton Overhauser experiments on kringle 4 from human plasminogen. Implications for the structure of the kringles' hydrophobic core.
[7]
PubMed ID4041537
JournalBiophys J
Year1985
Volume48
Pages411-22
AuthorsDe Marco A, Motta A, Llinas M, Laursen RA
TitleMacro- and micro-stabilities of the kringle 4 domain from plasminogen. The effect of ligand binding.
[8]
PubMed ID3004350
JournalArch Biochem Biophys
Year1986
Volume244
Pages727-41
AuthorsDe Marco A, Laursen RA, Llinas M
Title1H-NMR spectroscopic manifestations of ligand binding to the kringle 4 domain of human plasminogen.
[9]
PubMed ID3803570
JournalFEBS Lett
Year1986
Volume209
Pages111-6
AuthorsWilliams RJ, Esnouf P, Lawrence M, Cederholm-Williams SA
TitleThe similarities and differences in structures between kringle 1 of prothrombin and kringle 4 of plasminogen.
[10]
PubMed ID3531210
JournalJ Biol Chem
Year1986
Volume261
Pages13684-92
AuthorsMotta A, Laursen RA, Rajan N, Llinas M
TitleProton magnetic resonance study of kringle 1 from human plasminogen. Insights into the domain structure.
[11]
PubMed ID2820478
JournalBiochemistry
Year1987
Volume26
Pages3827-36
AuthorsMotta A, Laursen RA, Llinas M, Tulinsky A, Park CH
TitleComplete assignment of the aromatic proton magnetic resonance spectrum of the kringle 1 domain from human plasminogen: structure of the ligand-binding site.
[12]
PubMed ID3030435
JournalBiochim Biophys Acta
Year1987
Volume912
Pages254-69
AuthorsThewes T, Ramesh V, Simplaceanu EL, Llinas M
TitleIsolation, purification and 1H-NMR characterization of a kringle 5 domain fragment from human plasminogen.
[13]
PubMed ID2828641
JournalJ Mol Biol
Year1987
Volume198
Pages481-98
AuthorsRamesh V, Petros AM, Llinas M, Tulinsky A, Park CH
TitleProton magnetic resonance study of lysine-binding to the kringle 4 domain of human plasminogen. The structure of the binding site.
[14]
PubMed ID2954262
JournalThromb Res
Year1987
Volume45
Pages451-62
AuthorsHijikata-Okunomiya A, Okamoto S, Kikumoto R, Tamao Y, Ohkubo K, Tezuka T, Tonomura S, Matsumoto O
TitleSimilarity and dissimilarity in the stereogeometry of the active sites of thrombin, trypsin, plasmin and glandular kallikrein.
[15]
PubMed ID3338450
JournalEur J Biochem
Year1988
Volume170
Pages539-48
AuthorsMabbutt BC, Williams RJ
TitleTwo-dimensional 1H-NMR studies of the solution structure of plasminogen kringle 4.
[16]
PubMed ID2841130
JournalEur J Biochem
Year1988
Volume175
Pages237-49
AuthorsThewes T, Ramesh V, Simplaceanu EL, Llinas M
TitleAnalysis of the aromatic 1H-NMR spectrum of the kringle 5 domain from human plasminogen. Evidence for a conserved kringle fold.
[17]
PubMed ID3135547
JournalProteins
Year1988
Volume3
Pages85-96
AuthorsTulinsky A, Park CH, Mao B, Llinas M
TitleLysine/fibrin binding sites of kringles modeled after the structure of kringle 1 of prothrombin.
[18]
PubMed ID2535939
JournalBiochim Biophys Acta
Year1989
Volume994
Pages121-37
AuthorsDe Marco A, Petros AM, Llinas M, Kaptein R, Boelens R
TitleLigand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy.
[19]
PubMed ID1966798
JournalBlood Coagul Fibrinolysis
Year1990
Volume1
Pages673-9
AuthorsMulichak AM, Tulinsky A
TitleStructure of the lysine-fibrin binding subsite of human plasminogen kringle 4.
[20]
PubMed ID2105955
JournalJ Biol Chem
Year1990
Volume265
Pages3906-15
AuthorsThewes T, Constantine K, Byeon IJ, Llinas M
TitleLigand interactions with the kringle 5 domain of plasminogen. A study by 1H NMR spectroscopy.
[21]
CommentsSTRUCTURE BY NMR OF 374-461.
Medline ID90219023
PubMed ID2157850
JournalJ Mol Biol
Year1990
Volume212
Pages541-52
AuthorsAtkinson RA, Williams RJ
TitleSolution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry.
Related Swiss-protP00747
[22]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 374-461.
Medline ID92031502
PubMed ID1657148
JournalBiochemistry
Year1991
Volume30
Pages10576-88
AuthorsMulichak AM, Tulinsky A, Ravichandran KG
TitleCrystal and molecular structure of human plasminogen kringle 4 refined at 1.9-A resolution.
Related PDB1pk4
Related Swiss-protP00747
[23]
CommentsX-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 374-461.
Medline ID92031503
PubMed ID1657149
JournalBiochemistry
Year1991
Volume30
Pages10589-94
AuthorsWu TP, Padmanabhan K, Tulinsky A, Mulichak AM
TitleThe refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4.
Related PDB2pk4
Related Swiss-protP00747
[24]
PubMed ID1847112
JournalFEBS Lett
Year1991
Volume278
Pages17-22
AuthorsTeuten AJ, Smith RA, Dobson CM
TitleDomain interactions in human plasminogen studied by proton NMR.
[25]
PubMed ID1827215
JournalThromb Haemost
Year1991
Volume65
Pages67-72
AuthorsLu H, Soria C, Li H, Soria J, Lijnen HR, Perrot JY, Caen JP
TitleRole of active center and lysine binding sites of plasmin in plasmin-induced platelet activation and disaggregation.
[26]
PubMed ID1533399
JournalJ Cell Physiol
Year1992
Volume151
Pages255-61
AuthorsRyan TJ, Lai L, Malik AB
TitlePlasmin generation induces neutrophil aggregation: dependence on the catalytic and lysine binding sites.
[27]
PubMed ID8218159
JournalBiochemistry
Year1993
Volume32
Pages10936-43
AuthorsHoover GJ, Menhart N, Martin A, Warder S, Castellino FJ
TitleAmino acids of the recombinant kringle 1 domain of human plasminogen that stabilize its interaction with omega-amino acids.
[28]
CommentsX-ray crystallography
PubMed ID8054447
JournalBlood Coagul Fibrinolysis
Year1994
Volume5
Pages157-66
AuthorsWu TP, Padmanabhan KP, Tulinsky A
TitleThe structure of recombinant plasminogen kringle 1 and the fibrin binding site.
Related PDB1pkr
[29]
PubMed ID8187244
JournalChem Phys Lipids
Year1994
Volume67-68
Pages43-58
AuthorsCox M, Schaller J, Boelens R, Kaptein R, Rickli E, Llinas M
TitleKringle solution structures via NMR: two-dimensional 1H-NMR analysis of horse plasminogen kringle 4.
[30]
CommentsSTRUCTURE BY NMR OF 96-184.
Medline ID94237158
PubMed ID8181476
JournalEur J Biochem
Year1994
Volume221
Pages939-49
AuthorsRejante MR, Llinas M
TitleSolution structure of the epsilon-aminohexanoic acid complex of human plasminogen kringle 1.
Related PDB1hpj,1hpk
Related Swiss-protP00747
[31]
CommentsSTRUCTURE BY NMR OF 96-184.
Medline ID94237157
PubMed ID8181475
JournalEur J Biochem
Year1994
Volume221
Pages927-37
AuthorsRejante MR, Llinas M
Title1H-NMR assignments and secondary structure of human plasminogen kringle 1.
Related Swiss-protP00747
[32]
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
[33]
PubMed ID7793622
JournalAnal Biochem
Year1995
Volume226
Pages225-31
AuthorsCastro MJ, Kingston IB, Anderson S
TitleA spectrophotometric assay for the determination of the catalytic efficiency of plasminogen activators using a slowly hydrolyzed plasmin substrate.
[34]
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.
[35]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 102-181.
Medline ID96180681
PubMed ID8611560
JournalBiochemistry
Year1996
Volume35
Pages2567-76
AuthorsMathews II, Vanderhoff-Hanaver P, Castellino FJ, Tulinsky A
TitleCrystal structures of the recombinant kringle 1 domain of human plasminogen in complexes with the ligands epsilon-aminocaproic acid and trans-4-(aminomethyl)cyclohexane-1-carboxylic Acid.
Related PDB1cea,1ceb
Related Swiss-protP00747
[36]
CommentsSTRUCTURE BY NMR OF 183-354.
Medline ID96194156
PubMed ID8652577
JournalBiochemistry
Year1996
Volume35
Pages2357-64
AuthorsSohndel S, Hu CK, Marti D, Affolter M, Schaller J, Llinas M, Rickli EE
TitleRecombinant gene expression and 1H NMR characteristics of the kringle (2 + 3) supermodule: spectroscopic/functional individuality of plasminogen kringle domains.
Related Swiss-protP00747
[37]
CommentsX-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 376-454
JournalActa Crystallogr D Biol Crystallogr
Year1997
Volume53
Pages169-78
AuthorsStec B, Yamano A, Whitlow M, Teeter MM
TitleStructure of Human Plasminogen Kringle 4 at 1.68 angstrom and 277 K. A Possible Structural Role of Disordered Residues.
Related PDB1krn
Related Swiss-protP00747
[38]
CommentsPHOSPHORYLATION SITE SER-597.
Medline ID97345939
PubMed ID9201958
JournalBiochemistry
Year1997
Volume36
Pages8100-6
AuthorsWang H, Prorok M, Bretthauer RK, Castellino FJ
TitleSerine-578 is a major phosphorylation locus in human plasma plasminogen.
Related Swiss-protP00747
[39]
CommentsX-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 480-563.
Medline ID98198034
PubMed ID9521645
JournalBiochemistry
Year1998
Volume37
Pages3258-71
AuthorsChang Y, Mochalkin I, McCance SG, Cheng B, Tulinsky A, Castellino FJ
TitleStructure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen.
Related PDB5hpg
Related Swiss-protP00747
[40]
PubMed ID9563511
JournalFEBS Lett
Year1998
Volume425
Pages448-52
AuthorsTakeda-Shitaka M, Umeyama H
TitleElucidation of the cause for reduced activity of abnormal human plasmin containing an Ala55-Thr mutation: importance of highly conserved Ala55 in serine proteases.
[41]
CommentsX-ray crystallography
PubMed ID9783753
JournalNat Struct Biol
Year1998
Volume5
Pages917-23
AuthorsParry MA, Fernandez-Catalan C, Bergner A, Huber R, Hopfner KP, Schlott B, Guhrs KH, Bode W
TitleThe ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action.
Related PDB1bui
[42]
PubMed ID9761475
JournalProtein Sci
Year1998
Volume7
Pages1947-59
AuthorsAn SS, Marti DN, Carreno C, Albericio F, Schaller J, Llinas M
TitleStructural/functional properties of the Glu1-HSer57 N-terminal fragment of human plasminogen: conformational characterization and interaction with kringle domains.
[43]
CommentsX-ray crystallography
PubMed ID9733510
JournalScience
Year1998
Volume281
Pages1662-5
AuthorsWang X, Lin X, Loy JA, Tang J, Zhang XC
TitleCrystal structure of the catalytic domain of human plasmin complexed with streptokinase.
Related PDB1bml
[44]
CommentsNMR Structure
PubMed ID10625440
JournalBiochemistry
Year1999
Volume38
Pages15741-55
AuthorsMarti DN, Schaller J, Llinas M
TitleSolution structure and dynamics of the plasminogen kringle 2-AMCHA complex: 3(1)-helix in homologous domains.
Related PDB1b2i
[45]
CommentsX-ray crystallography
PubMed ID10460175
JournalBiochemistry
Year1999
Volume38
Pages11180-8
AuthorsPeisach E, Wang J, de los Santos T, Reich E, Ringe D
TitleCrystal structure of the proenzyme domain of plasminogen.
Related PDB1qrz
[46]
PubMed ID10390345
JournalJ Mol Biol
Year1999
Volume290
Pages471-9
AuthorsJespers L, Lijnen HR, Vanwetswinkel S, Van Hoef B, Brepoels K, Collen D, De Maeyer M
TitleGuiding a docking mode by phage display: selection of correlated mutations at the staphylokinase-plasmin interface.
[47]
PubMed ID11076540
JournalBiochemistry
Year2000
Volume39
Pages13974-81
AuthorsBoxrud PD, Bock PE
TitleStreptokinase binds preferentially to the extended conformation of plasminogen through lysine binding site and catalytic domain interactions.
[48]
PubMed ID10769130
JournalBiochemistry
Year2000
Volume39
Pages4740-5
AuthorsLin LF, Houng A, Reed GL
TitleEpsilon amino caproic acid inhibits streptokinase-plasminogen activator complex formation and substrate binding through kringle-dependent mechanisms.
[49]
CommentsX-ray crystallography
PubMed ID10656799
JournalJ Mol Biol
Year2000
Volume295
Pages903-14
AuthorsWang X, Terzyan S, Tang J, Loy JA, Lin X, Zhang XC
TitleHuman plasminogen catalytic domain undergoes an unusual conformational change upon activation.
Related PDB1ddj
[50]
PubMed ID10926513
JournalJ Mol Biol
Year2000
Volume301
Pages333-47
AuthorsZajicek J, Chang Y, Castellino FJ
TitleThe effects of ligand binding on the backbone dynamics of the kringle 1 domain of human plasminogen.
[51]
PubMed ID11152303
JournalJ Pept Res
Year2000
Volume56
Pages438-45
AuthorsSchenone MM, Warder SE, Martin JA, Prorok M, Castellino FJ
TitleAn internal histidine residue from the bacterial surface protein, PAM, mediates its binding to the kringle-2 domain of human plasminogen.
[52]
CommentsX-ray crystallography
PubMed ID11350170
JournalJ Mol Biol
Year2001
Volume308
Pages705-19
AuthorsRios-Steiner JL, Schenone M, Mochalkin I, Tulinsky A, Castellino FJ
TitleStructure and binding determinants of the recombinant kringle-2 domain of human plasminogen to an internal peptide from a group A Streptococcal surface protein.
Related PDB1i5k
[53]
PubMed ID12080056
JournalJ Biol Chem
Year2002
Volume277
Pages33068-74
AuthorsTurner RB, Liu L, Sazonova IY, Reed GL
TitleStructural elements that govern the substrate specificity of the clot-dissolving enzyme plasmin.
[54]
CommentsX-ray crystallography
PubMed ID12054798
JournalJ Mol Biol
Year2002
Volume318
Pages1009-17
AuthorsAbad MC, Arni RK, Grella DK, Castellino FJ, Tulinsky A, Geiger JH
TitleThe X-ray crystallographic structure of the angiogenesis inhibitor angiostatin.
Related PDB1ki0
[55]
CommentsX-ray crystallography
PubMed ID12456874
JournalProtein Eng
Year2002
Volume15
Pages753-61
AuthorsWakeham N, Terzyan S, Zhai P, Loy JA, Tang J, Zhang XC
TitleEffects of deletion of streptokinase residues 48-59 on plasminogen activation.
Related PDB1l4d
[56]
PubMed ID12515545
JournalBiochemistry
Year2003
Volume42
Pages114-20
AuthorsZhai P, Wakeham N, Loy JA, Zhang XC
TitleFunctional roles of streptokinase C-terminal flexible peptide in active site formation and substrate recognition in plasminogen activation.
[57]
PubMed ID12773528
JournalJ Biol Chem
Year2003
Volume278
Pages30569-77
AuthorsSundram V, Nanda JS, Rajagopal K, Dhar J, Chaudhary A, Sahni G
TitleDomain truncation studies reveal that the streptokinase-plasmin activator complex utilizes long range protein-protein interactions with macromolecular substrate to maximize catalytic turnover.
[58]
CommentsX-ray crystallography
PubMed ID15211511
JournalProteins
Year2004
Volume56
Pages277-84
AuthorsTerzyan S, Wakeham N, Zhai P, Rodgers K, Zhang XC
TitleCharacterization of Lys-698-to-Met substitution in human plasminogen catalytic domain.
Related PDB1rjx

comments
This enzyme is composed of N-terminal PAN domain, five kringle domains and trypsin-like serine protease domain. This enzyme is activated by Streptokinase.
Although this enzyme has got a classical catalytic triad, composed of Ser/His/Asp, which is the same as that of trypsin, its oxyanion hole is not catalytically competent, according to literature [49].
Thus, it should not be included in the same classification with trypsin (D00197 in EzCatDB).

createdupdated
2004-08-202011-02-17


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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