Theoretical studies on the deacylation step of acylated Candida Antarctica lipase B: structural and reaction pathway analysis.

Clicks: 257
ID: 38275
2015
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Abstract
The deacylation step of acylated Candida Antarctica lipase B, which was acylated with methylcaprylate (MEC) and acetylcholine (ACh), has been studied by using density functional theory method. Free energies of the entire reaction were calculated for enzyme deacylation by water and hydrogen peroxide that represented hydrolysis and perhydrolysis reactions, respectively. The calculations displayed that a stepwise mechanism there was with the enzyme-product complex being a deep minimum on the free energy surfaces of both of two reactions. The tetrahedral intermediate formation was the rate-determining step of all reactions, which needed 8.1 to 10.5kcalmol(-1) for activation in different reactions. In the second stage of the reaction, fewer free energy barriers, between 4.7 and 5.9kcalmol(-1), were identified to enable the proton transfer from His224 to Ser105 and the breakdown of the tetrahedral intermediate. These calculated activation free energies approved theoretical possibility of both of two reactions for two substrates. Finally, an applied tool examined the interactions role in the stability and energy levels of different chemical species.
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sadeghi-googheri2015theoreticaljournal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Sadeghi Googheri, Mohammad Sadegh;Housaindokht, Mohammad Reza;Sabzyan, Hassan;
Journal journal of molecular graphics & modelling
Year 2015
DOI
10.1016/j.jmgm.2015.01.003
URL
Keywords Keywords not found

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