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Identification
NameStreptokinase
Accession NumberDB00086  (BIOD00028, BTD00028)
Typebiotech
Groupsapproved
Description

Streptokinase, is a sterile, purified preparation of a bacterial protein elaborated by group C (beta) -hemolytic streptococci.

Protein structureDb00086
Protein chemical formulaC2100H3278N566O669S4
Protein average weight47286.7000
Sequences
>Streptokinase Sequence DB00086
MKNYLSFGMFALLFALTFGTVNSVQAIAGPEWLLDRPSVNNSQLVVSVAGTVEGTNQDIS
LKFFEIDLTSRPAHGGKTEQGLSPKSKPFATDSGAMSHKLEKADLLKAIQEQLIANVHSN
DDYFEVIDFASDATITDRNGKVYFADKDGSVTLPTQPVQEFLLSGHVRVRPYKEKPIQNQ
AKSVDVEYTVQFTPLNPDDDFRPGLKDTKLLKTLAIGDTITSQELLAQAQSILNKNHPGY
TIYERDSSIVTHDNDIFRTILPMDQEFTYRVKNREQAYRINKKSGLNEEINNTDLISEKY
YVLKKGEKPYDPFDRSHLKLFTIKYVDVDTNELLKSEQLLTASERNLDFRDLYDPRDKAK
LLYNNLDAFGIMDYTLTGKVEDNHDDTNRIITVYMGKRPEGENASYHLAYDKDRYTEEER
EVYSYLRYTGTPIPDNPNDK
Download FASTA Format
Synonyms
SynonymLanguageCode
Streptokinase C precursorNot AvailableNot Available
SaltsNot Available
Brand names
NameCompany
StreptaseAventis Behringer GmbH
Brand mixturesNot Available
Categories
CAS number9002-01-1
Taxonomy
KingdomOrganic Compounds
SuperclassOrganic Acids
ClassCarboxylic Acids and Derivatives
SubclassAmino Acids, Peptides, and Analogues
Direct parentPeptides
Alternative parentsNot Available
SubstituentsNot Available
Classification descriptionNot Available
Pharmacology
IndicationFor the treatment of acute evolving transmural myocardial infarction, pulmonary embolism, deep vein thrombosis, arterial thrombosis or emolism and occlusion of arteriovenous cannulae
PharmacodynamicsStreptokinase creates an active complex which promotes the cleavage of the Arg/Val bond in plasminogen to form the proteolytic enzyme plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction.
Mechanism of actionPlasminogen 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.
AbsorptionNot Available
Volume of distributionNot Available
Protein bindingNot Available
Metabolism
Route of eliminationNot Available
Half lifeNot Available
ClearanceNot Available
ToxicityNot Available
Affected organisms
  • Humans and other mammals
Pathways
PathwayCategorySMPDB ID
Streptokinase Action PathwayDrug actionSMP00282
SNP Mediated EffectsNot Available
SNP Mediated Adverse Drug ReactionsNot Available
Pharmacoeconomics
ManufacturersNot Available
Packagers
Dosage forms
FormRouteStrength
Powder, for solutionIntravenous
PricesNot Available
PatentsNot Available
Properties
Stateliquid
Experimental Properties
PropertyValueSource
hydrophobicity-0.728Not Available
isoelectric point5.12Not Available
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.

US6087332
General ReferenceNot Available
External Links
ResourceLink
UniProtP00779
GenbankK02986
PharmGKBPA164754919
Drug Product Database2018993
RxListhttp://www.rxlist.com/cgi/generic2/streptokinase.htm
Drugs.comhttp://www.drugs.com/cons/streptokinase-intravenous-intracoronary.html
WikipediaStreptokinase
ATC CodesB01AD01B06AA55
AHFS Codes
  • 20:12.20
PDB Entries
FDA labelNot Available
MSDSNot Available
Interactions
Drug Interactions
Drug
TiclopidineIncreased bleeding risk. Monitor for signs of bleeding.
Food InteractionsNot Available

Targets

1. Plasminogen

Kind: protein

Organism: Human

Pharmacological action: yes

Actions: activator

Components

Name UniProt ID Details
Plasminogen P00747 Details

References:

  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. Pubmed
  2. Alessi MC, Juhan-Vague I: [Thrombolytics and their use] Rev Prat. 1999 Oct 1;49(15):1654-8. Pubmed
  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. Pubmed
  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. Pubmed
  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. Pubmed
  6. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. Pubmed

2. Proteinase-activated receptor 1

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cleavage

Components

Name UniProt ID Details
Proteinase-activated receptor 1 P25116 Details

References:

  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. Pubmed

Enzymes

1. Cytosolic phospholipase A2

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: inducer

Components

Name UniProt ID Details
Cytosolic phospholipase A2 P47712 Details

References:

  1. Kawaguchi H, Iizuka K, Sano H, Yasuda H: Effect of streptokinase on prostacyclin synthesis and phospholipase activity in cultured pulmonary artery endothelial cells. Biochim Biophys Acta. 1990 Dec 10;1055(3):223-9. Pubmed

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Drug created on June 13, 2005 07:24 / Updated on September 13, 2013 10:49