Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?
AbstractCandida 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
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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.
Bordes I, Recatalá J, Świderek K, Moliner V. Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? Molecules. 2015; 20(10):17789-17806.Chicago/Turabian Style
Bordes, Isabel; Recatalá, José; Świderek, Katarzyna; Moliner, Vicent. 2015. "Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?" Molecules 20, no. 10: 17789-17806.