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Literature summary for 3.4.21.5 extracted from

  • De Cristofaro, R.; De Candia, E.
    Thrombin domains: structure, function and interaction with platelet receptors (2003), J. Thromb. Thrombolysis, 15, 151-163.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
factor V + H2O Homo sapiens proteolytic activation factor Va + propeptide
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?
factor VIII + H2O Homo sapiens proteolytic activation factor VIIIa + propeptide
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?
factor XI + H2O Homo sapiens proteolytic activation factor XIa + propeptide
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?
factor XIII + H2O Homo sapiens proteolytic activation factor XIIIa + propeptide
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?
fibrinogen + H2O Homo sapiens proteolytic activation fibrin + fibrinopeptide A + fibrinopeptide B
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?
additional information Homo sapiens enzyme plays a pivotal role in hemostasis, thrombosis, cell differentiation, and is involved in the activation of many cell types and platelets ?
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Reaction

Reaction Comment Organism Reaction ID
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B catalytic tetrad, composed of His57, Asp102, Ser195, and Ser214, at the bottom of a canyon-like cleft shaping the catalytic pocket, further regulation of specificity by recognition domains along with insertion loops Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
factor V + H2O proteolytic activation Homo sapiens factor Va + propeptide
-
?
factor VIII + H2O proteolytic activation Homo sapiens factor VIIIa + propeptide
-
?
factor XI + H2O proteolytic activation Homo sapiens factor XIa + propeptide
-
?
factor XIII + H2O proteolytic activation Homo sapiens factor XIIIa + propeptide
-
?
fibrinogen + H2O proteolytic activation Homo sapiens fibrin + fibrinopeptide A + fibrinopeptide B
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?
fibrinogen + H2O proteolytic activation Homo sapiens fibrin + fibrinopeptide A + fibrinopeptide B fibrinopeptide A D49 binds to thrombin R67 ?
additional information determination of residues involved in ligand binding, overview, interaction with receptors glycoprotein Ibalpha GpIb and protease-activated receptor I PARI in platelet membrane, thrombin recognition domains and insertion loops are responsible for substrate specificity determination and interaction with inhibitors, unique within serine proteases, thrombin can be at the same time very efficient and specific for different substrates and inhibitors, overview Homo sapiens ?
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?
additional information enzyme plays a pivotal role in hemostasis, thrombosis, cell differentiation, and is involved in the activation of many cell types and platelets Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More structure analysis, 2 of several recognition domains are the fibrinogen recognition site or anion binding exosite I formed by a loop of residues Arg67-Ile82, and the heparin binding site or anion binding exosite II localized at the C-terminus of the B-chain, localization and structure of recognition sites and insertion loops within the enzyme molecule, interaction with ligands, receptors and substrates, overview Homo sapiens