ENZO URL:

<p><a href="http://enzo.cmm.ki.si" target="_blank">http://enzo.cmm.ki.si</a><b>.</b> The ENZO web page provides a short introduction and links to a quick guide, examples and ENZO tool.</p

Enzyme titration reaction scheme.

<p>E is the <i>Torpedo californica</i> acetylcholinesterase enzyme, I the m-(N,N,N-trimethylammonio) trifluoroacetophenone (TMTFA) inhibitor, and EI their complex; <i>k₀</i> is a second order association rate constant. The reaction was drawn using the <i>Reaction Scheme</i> tab of ENZO.</p

Michaelis-Menten reaction scheme.

<p>E is the free enzyme, S the substrate, ES the Michaelis complex and P the product; <i>k₀</i> is a second order and <i>k₁</i> and <i>k₂</i> are first order rate constants, respectively. The differential equations were automatically generated from the drawn reaction scheme by ENZO.</p

Converged results of parameter fitting for enzyme active site titration experiment.

<p>Initial concentrations of enzyme E and inhibitor I for progress curve files tfk1.dat, tfk2.dat, tfk3.dat (<i>Experimental Data</i> panel shows tfk1.dat) are fitted in the interval of [0, 10²⁰]; the initial concentration of EI is zero and fixed; the checkbox “E” is checked under <i>Measured Species</i>, which signifies that E is the measured quantity and the progress curves below represent the time course of its residual activity. The respective units of the residual activity in the Y-axis are OD/min and the units of time in X-axis are seconds. Fitted rate constant <i>k₀</i> and initial values of E and I at three different concentrations of I are displayed under the <i>Evaluated Parameters</i> in the upper right corner panel, the experimental progress curves are blue and the fitted curves are red as shown in <i>Time Course of the Reaction</i> chart at the bottom panel of the screen. The arrows mark the difference between the inital value and the plateau.</p