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. Author manuscript; available in PMC: 2014 Jun 1.
Published in final edited form as: J Thromb Haemost. 2013 Jun;11(0 1):265–276. doi: 10.1111/jth.12217

Figure 3. Multi-step Pathway for Protein Substrate Recognition by Prothrombinase.

Figure 3

Kinetic scheme resolved for the action of prothrombinase on P2. The initial binding interaction between substrate (S) and prothrombinase (E) to form ES results from exosite-dependent interactions between S and E. Exosite binding is followed by a unimolecular binding step in which structures flanking the cleavage site engage the active-site of the enzyme before catalysis can occur. The product (P) is also bound to E by exosite interactions before it is released. The graphical legend highlights the important features of S and E. The composite nature of the steady state kinetic constants is illustrated by derivation employing the rapid equilibrium assumption. Ks* is defined as [E.S]/[E.S*].