Sandbox Reserved 1852: Difference between revisions

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[[Image:DAcombinedkineticdata Large.jpeg|700px|left|thumb|Figure 4. A) Catalytic efficiencies of key Diels-Alderase generations. Kinetic data was measured at 25°C, in PBS, at pH 7.4. B) Improvement of catalytic efficiency across generations.<ref name="Preiswerk">PMID:24847076</ref>]]

Classic [https://en.wikipedia.org/wiki/Michaelis%E2%80%93Menten_kinetics Michaelis-Menten kinetics]were determined for each generation of the enzyme. As the Diels-Alderase relies on a catalyzed interaction between both the diene and dienophile, a Michaelis binding constant (''K<sub>m</sub>'' value) was determined for each substrate separately before catalytic efficiency was calculated. The CE20 model of the enzyme is over 300-fold more efficient than the first enzyme model due to increasing active site specificity [Fig. 4].<ref name="Preiswerk"/>

Classic [https://en.wikipedia.org/wiki/Michaelis%E2%80%93Menten_kinetics Michaelis-Menten kinetics]were determined for each generation of the enzyme. As the Diels-Alderase relies on a catalyzed interaction between both the diene and dienophile, a Michaelis binding constant (''K<sub>m</sub>'' value) was determined for each substrate separately before catalytic efficiency was calculated. The CE20 model of the enzyme is over 300-fold more efficient than the first enzyme model due to increasing active site specificity [Fig. 4].<ref name="Preiswerk"/> The authors did not publish comparisons to free reflux originally.

Sandbox Reserved 1852: Difference between revisions

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Revision as of 18:55, 28 April 2025 view source Micah Zile (talk \| contribs) 78 edits No edit summary ← Older edit		Revision as of 18:57, 28 April 2025 view source Micah Zile (talk \| contribs) 78 edits No edit summary Newer edit →
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	[[Image:DAcombinedkineticdata Large.jpeg\|700px\|left\|thumb\|Figure 4. A) Catalytic efficiencies of key Diels-Alderase generations. Kinetic data was measured at 25°C, in PBS, at pH 7.4. B) Improvement of catalytic efficiency across generations.<ref name="Preiswerk">PMID:24847076</ref>]]		[[Image:DAcombinedkineticdata Large.jpeg\|700px\|left\|thumb\|Figure 4. A) Catalytic efficiencies of key Diels-Alderase generations. Kinetic data was measured at 25°C, in PBS, at pH 7.4. B) Improvement of catalytic efficiency across generations.<ref name="Preiswerk">PMID:24847076</ref>]]

	Classic [https://en.wikipedia.org/wiki/Michaelis%E2%80%93Menten_kinetics Michaelis-Menten kinetics]were determined for each generation of the enzyme. As the Diels-Alderase relies on a catalyzed interaction between both the diene and dienophile, a Michaelis binding constant (''K<sub>m</sub>'' value) was determined for each substrate separately before catalytic efficiency was calculated. The CE20 model of the enzyme is over 300-fold more efficient than the first enzyme model due to increasing active site specificity [Fig. 4].<ref name="Preiswerk"/>		Classic [https://en.wikipedia.org/wiki/Michaelis%E2%80%93Menten_kinetics Michaelis-Menten kinetics]were determined for each generation of the enzyme. As the Diels-Alderase relies on a catalyzed interaction between both the diene and dienophile, a Michaelis binding constant (''K<sub>m</sub>'' value) was determined for each substrate separately before catalytic efficiency was calculated. The CE20 model of the enzyme is over 300-fold more efficient than the first enzyme model due to increasing active site specificity [Fig. 4].<ref name="Preiswerk"/> The authors did not publish comparisons to free reflux originally.