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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





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Academic Editors: Diego A. Alonso and Isidro M. Pastor

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





Autor: Isabel Bordes 1, José Recatalá 1, Katarzyna Świderek 1,2,* and Vicent Moliner 1,*

Fuente: http://mdpi.com/



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