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. Author manuscript; available in PMC: 2007 Jul 1.
Published in final edited form as: FEBS J. 2006 Jun 5;273(13):2942–2954. doi: 10.1111/j.1742-4658.2006.05305.x

Figure 1.

Figure 1

Protease inhibition by the serpin mechanism. I, inhibitor (e.g. α1-antitrypsin); E, enzyme (e.g. trypsin); k1 and k−1 denote the forward and reverse rate constants of the formation of the non-covalent complex EI; k2 is the rate constant of the formation of the acyl-enzyme intermediate EI’; k3 is the rate constant of deacylation, resulting in free enzyme and inactivated, cleaved serpin I*; k4 is the rate constant of the formation of the kinetically trapped, stable covalent complex EI*; k5 is the dissociation rate constant of the covalent complex. Adapted with modifications from [11].