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Molecules 2015, 20(10), 17789-17806; doi:10.3390/molecules201017789

Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?

1
Departament de Química Física i Analítica, Universitat Jaume I, Castellón 12071, Spain
2
Institute of Applied Radiation Chemistry, Lodz University of Technology, Lodz 90-924, Poland
*
Authors to whom correspondence should be addressed.
Academic Editors: Diego A. Alonso and Isidro M. Pastor
Received: 7 August 2015 / Revised: 10 September 2015 / Accepted: 11 September 2015 / Published: 25 September 2015
(This article belongs to the Special Issue Phase-Transfer Catalysis)
View Full-Text   |   Download PDF [6484 KB, uploaded 25 September 2015]   |  

Abstract

Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrolase (sEH) formed by a nucleophile-histidine-acid catalytic triad and an oxyanion hole typical for molecular structures derived from processes of α/β hydrolases. In this work we are exploring these similarities and proposing a Ser105Asp variant of CALB as a new catalyst for epoxide hydrolysis. In particular, the hydrolysis of the trans-diphenylpropene oxide (t-DPPO) is studied by means of quantum cluster models mimicking the active site of both enzymes. Our results, based on semi-empirical and DFT calculations, suggest that mutant Ser105Asp CALB is a good protein scaffold to be used for the bio-synthesis of chiral compounds. View Full-Text
Keywords: Candida antarctica lipase B; CALB; epoxide hydrolase; sEH; reaction mechanism; trans-diphenylpropene oxide; enzyme promiscuity; catalysis; quantum cluster models Candida antarctica lipase B; CALB; epoxide hydrolase; sEH; reaction mechanism; trans-diphenylpropene oxide; enzyme promiscuity; catalysis; quantum cluster models
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Bordes, I.; Recatalá, J.; Świderek, K.; Moliner, V. Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? Molecules 2015, 20, 17789-17806.

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