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Record Information
Creation Date2014-09-11 05:13:41 UTC
Update Date2014-12-24 20:26:56 UTC
Accession NumberT3D4727
Common NameStreptokinase
DescriptionStreptokinase, is a sterile, purified preparation of a bacterial protein elaborated by group C (beta) -hemolytic streptococci.
Compound Type
  • Amide
  • Amine
  • Bacterial Toxin
  • Fibrinolytic Agent
  • Natural Compound
  • Organic Compound
  • Protein
  • Thrombolytic Agent
Protein StructureT3d4727
Streptokinase C precursor
Chemical FormulaNot Available
Average Molecular Mass50139.695 g/mol
CAS Registry Number9002-01-1
SequenceNot Available
Chemical Taxonomy
DescriptionNot Available
KingdomOrganic Compounds
Super ClassOrganic Acids
ClassCarboxylic Acids and Derivatives
Sub ClassAmino Acids, Peptides, and Analogues
Direct ParentPeptides
Alternative ParentsNot Available
SubstituentsNot Available
Molecular FrameworkNot Available
External DescriptorsNot Available
Biological Properties
StatusDetected and Not Quantified
Cellular LocationsNot Available
Biofluid LocationsNot Available
Tissue LocationsNot Available
PathwaysNot Available
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Physical Properties
AppearanceClear solution.
Experimental Properties
Melting PointNot Available
Boiling PointNot Available
Solubility>10 mg/mL
LogPNot Available
Predicted PropertiesNot Available
Spectrum TypeDescriptionSplash KeyView
Toxicity Profile
Route of ExposureOral
Mechanism of ToxicityPlasminogen is an inactive molecule that becomes activated to plasmin when the Arg/Val bond is cleaved. Plasmin breaks down fibrin clots created by the blood clotting cascade. Streptokinase forms a highly specific 1:1 enzymatic complex with plasminogen which converts inactive plasminogen molecules into active plasmin. Plasmin degrades fibrin clots as well as fibrinogen and other plasma proteins. This in turn leads to the degradation of blood clots.
MetabolismFree toxin may be removed by opsonization via the reticuloendothelial system (primarily the liver and kidneys) or it may be degraded through cellular internalization via the lysosomes. Lysosomes are membrane-enclosed organelles that contain an array of digestive enzymes, including several proteases.
Toxicity ValuesNot Available
Lethal DoseNot Available
Carcinogenicity (IARC Classification)No indication of carcinogenicity to humans (not listed by IARC).
Uses/SourcesFor the treatment of acute evolving transmural myocardial infarction, pulmonary embolism, deep vein thrombosis, arterial thrombosis or emolism and occlusion of arteriovenous cannulae
Minimum Risk LevelNot Available
Health EffectsNot Available
SymptomsNot Available
TreatmentNot Available
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDDB00086
HMDB IDNot Available
PubChem Compound IDNot Available
ChemSpider IDNot Available
KEGG IDNot Available
UniProt IDP00779
ChEBI IDNot Available
BioCyc IDNot Available
CTD IDNot Available
Stitch IDStreptokinase
ACToR IDNot Available
Wikipedia LinkStreptokinase
Synthesis Reference

Lawrence Isaac Galler, “Streptokinase derivatives with high affinity for activated platelets and methods of their production and use in thrombolytic therapy.” U.S. Patent US6087332, issued July, 1997.

General ReferencesNot Available
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated GenesNot Available


General Function:
Serine-type peptidase activity
Specific Function:
Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.
Gene Name:
Uniprot ID:
Molecular Weight:
90568.415 Da
  1. Caballero AR, Lottenberg R, Johnston KH: Cloning, expression, sequence analysis, and characterization of streptokinases secreted by porcine and equine isolates of Streptococcus equisimilis. Infect Immun. 1999 Dec;67(12):6478-86. [10569766 ]
  2. Alessi MC, Juhan-Vague I: [Thrombolytics and their use]. Rev Prat. 1999 Oct 1;49(15):1654-8. [10581996 ]
  3. Chaudhary A, Vasudha S, Rajagopal K, Komath SS, Garg N, Yadav M, Mande SC, Sahni G: Function of the central domain of streptokinase in substrate plasminogen docking and processing revealed by site-directed mutagenesis. Protein Sci. 1999 Dec;8(12):2791-805. [10631997 ]
  4. Parry MA, Zhang XC, Bode I: Molecular mechanisms of plasminogen activation: bacterial cofactors provide clues. Trends Biochem Sci. 2000 Feb;25(2):53-9. [10664583 ]
  5. Korol'chuk VI, Makohonenko IeM, Sederkhol'm-Vil'iams SA: [Plasminogen binding with decapeptide and polypeptide fragments of streptokinase]. Ukr Biokhim Zh. 1999 Sep-Oct;71(5):51-8. [10726310 ]
  6. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [11752352 ]
General Function:
Thrombin receptor activity
Specific Function:
High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development.
Gene Name:
Uniprot ID:
Molecular Weight:
47439.83 Da
  1. McRedmond JP, Harriott P, Walker B, Fitzgerald DJ: Streptokinase-induced platelet activation involves antistreptokinase antibodies and cleavage of protease-activated receptor-1. Blood. 2000 Feb 15;95(4):1301-8. [10666203 ]