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3.4.21.5: thrombin
This is an abbreviated version, for detailed information about thrombin, go to the full flat file.
Reaction
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B =
Synonyms
activated factor II, alpha-thrombin, alphaTh, beta-thrombin, blood-coagulation factor II, activated, blood-coagulation factor IIa, clotting factor IIa, EC 3.4.4.13, factor IIa, fibrinogenase, thrombase, thrombin, E, thrombin-C, thrombofort, topical, tropostasin
ECTree
3.4.21.5 thrombinAdvanced search results
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20
104
26591
154
446
31
1374
11
11
20
Metals Ions
Metals Ions on EC 3.4.21.5 - thrombin
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
K+
Na+
additional information
K+
-
two ion binding sites per enzyme molecule, binding structure, molecular basis of monovalent cation selectivity, overview, the K+-bound enzyme form shows key differences compared with the Na+-bound structure resulting in different kinetics of activation, overview
Na+
-
two ion binding sites per enzyme molecule, free thrombin is a Na+-selective enzyme, the K+-bound enzyme form shows key differences compared with the Na+-bound structure resulting in different kinetics of activation, binding structure, overview
Na+
-
two-step mechanism of Na+ binding to thrombin resolved by ultra-rapid kinetics
Na+
-
the activating effect of Na+ on thrombin is allosteric and depends on the conformational transition from a low activity Na+-free, slow form to a high activity Na+-bound, fast form, overview, the Na+-free enzyme is in inactive conformation, Trp215, Arg187, and Arg221are involved, Na+ binding kinetics of wild-type and mutant enzymes, overview
Na+
-
kinetic mechanism of Na+ binding to thrombin, stopped-flow measurements of intrinsic fluorescence, two-step mechanism with a rapid phase occurring within the dead time of the spectrometer followed by a single-exponential slow phase whose kobs decreases hyperbolically with increasing Na+ concentration, overview
Na+
-
Na+ activates thrombin by securing the correct orientation of the Glu192-Gly193 peptide bond, which is likely flipped in the absence of cation
additional information
-
mutants show reduced specificity for monovalent cations compared to the wild-type enzyme
additional information
-
the cation-free enzyme form assumes a conformation where the monovalent cation binding site is completely disordered, the S1 pocket is inaccessible to substrate and binding to exosite I is compromised by an unprecedented shift in the position of the autolysis loop
Information
