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Literature summary for 3.4.21.5 extracted from

  • Winquist, J.; Geschwindner, S.; Xue, Y.; Gustavsson, L.; Musil, D.; Deinum, J.; Danielson, U.H.
    Identification of structural-kinetic and structural-thermodynamic relationships for thrombin inhibitors (2013), Biochemistry, 52, 613-626.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
melagatran effect of introducing substituted amine residues with increased chain length in the P3 residue of melagatran. The association rate becomes faster when the lipophilicity of the inhibitors is increased. This is coupled to an increased enthalpic component and a corresponding decreased entropic component. The dissociation rates are reduced with an increase in chain length, with only a smaller increase and a decrease in the enthalpic and entropic components, respectively. The affinity increases with an increase in chain length, with similar changes in the enthalpic and entropic components. The interaction of melagatran is the most enthalpy-driven interaction. The orientation of the P1 and P2 parts of the molecules is very similar, but there are significant differences in the interaction between the terminal part of the P3 side chain and the binding pocket Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Homo sapiens
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plasma
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
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 Homo sapiens D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
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