Streptokinase (T3D4727)
Record Information | |||||||||||
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Version | 2.0 | ||||||||||
Creation Date | 2014-09-11 05:13:41 UTC | ||||||||||
Update Date | 2014-12-24 20:26:56 UTC | ||||||||||
Accession Number | T3D4727 | ||||||||||
Identification | |||||||||||
Common Name | Streptokinase | ||||||||||
Class | Protein | ||||||||||
Description | Streptokinase, is a sterile, purified preparation of a bacterial protein elaborated by group C (beta) -hemolytic streptococci. | ||||||||||
Compound Type |
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Protein Structure | |||||||||||
Synonyms |
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Chemical Formula | Not Available | ||||||||||
Average Molecular Mass | 50139.695 g/mol | ||||||||||
CAS Registry Number | 9002-01-1 | ||||||||||
Sequence | Not Available | ||||||||||
Chemical Taxonomy | |||||||||||
Description | Not Available | ||||||||||
Kingdom | Organic Compounds | ||||||||||
Super Class | Organic Acids | ||||||||||
Class | Carboxylic Acids and Derivatives | ||||||||||
Sub Class | Amino Acids, Peptides, and Analogues | ||||||||||
Direct Parent | Peptides | ||||||||||
Alternative Parents | Not Available | ||||||||||
Substituents | Not Available | ||||||||||
Molecular Framework | Not Available | ||||||||||
External Descriptors | Not Available | ||||||||||
Biological Properties | |||||||||||
Status | Detected and Not Quantified | ||||||||||
Origin | Exogenous | ||||||||||
Cellular Locations | Not Available | ||||||||||
Biofluid Locations | Not Available | ||||||||||
Tissue Locations | Not Available | ||||||||||
Pathways | Not Available | ||||||||||
Applications | Not Available | ||||||||||
Biological Roles | Not Available | ||||||||||
Chemical Roles | Not Available | ||||||||||
Physical Properties | |||||||||||
State | Liquid | ||||||||||
Appearance | Clear solution. | ||||||||||
Experimental Properties |
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Predicted Properties | Not Available | ||||||||||
Spectra | |||||||||||
Spectra |
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Toxicity Profile | |||||||||||
Route of Exposure | Oral | ||||||||||
Mechanism of Toxicity | Plasminogen 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. | ||||||||||
Metabolism | Free 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 Values | Not Available | ||||||||||
Lethal Dose | Not Available | ||||||||||
Carcinogenicity (IARC Classification) | No indication of carcinogenicity to humans (not listed by IARC). | ||||||||||
Uses/Sources | For the treatment of acute evolving transmural myocardial infarction, pulmonary embolism, deep vein thrombosis, arterial thrombosis or emolism and occlusion of arteriovenous cannulae | ||||||||||
Minimum Risk Level | Not Available | ||||||||||
Health Effects | Not Available | ||||||||||
Symptoms | Not Available | ||||||||||
Treatment | Not Available | ||||||||||
Normal Concentrations | |||||||||||
Not Available | |||||||||||
Abnormal Concentrations | |||||||||||
Not Available | |||||||||||
External Links | |||||||||||
DrugBank ID | DB00086 | ||||||||||
HMDB ID | Not Available | ||||||||||
PubChem Compound ID | Not Available | ||||||||||
ChEMBL ID | CHEMBL2108147 | ||||||||||
ChemSpider ID | Not Available | ||||||||||
KEGG ID | Not Available | ||||||||||
UniProt ID | P00779 | ||||||||||
OMIM ID | |||||||||||
ChEBI ID | Not Available | ||||||||||
BioCyc ID | Not Available | ||||||||||
CTD ID | Not Available | ||||||||||
Stitch ID | Streptokinase | ||||||||||
PDB ID | 1BML | ||||||||||
ACToR ID | Not Available | ||||||||||
Wikipedia Link | Streptokinase | ||||||||||
References | |||||||||||
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. | ||||||||||
MSDS | T3D4727.pdf | ||||||||||
General References | Not Available | ||||||||||
Gene Regulation | |||||||||||
Up-Regulated Genes | Not Available | ||||||||||
Down-Regulated Genes | Not Available |
Targets
- 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:
- PLG
- Uniprot ID:
- P00747
- Molecular Weight:
- 90568.415 Da
References
- 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 ]
- Alessi MC, Juhan-Vague I: [Thrombolytics and their use]. Rev Prat. 1999 Oct 1;49(15):1654-8. [10581996 ]
- 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 ]
- 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 ]
- 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 ]
- 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:
- F2R
- Uniprot ID:
- P25116
- Molecular Weight:
- 47439.83 Da
References
- 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 ]