Substrate Specificity of the Highly Thermostable Esterase EstDZ3 |
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Authors: | Angelos Papanikolaou Dr Alexandra V Chatzikonstantinou Dr Dimitra Zarafeta Prof Nikolaos Kourkoumelis Dr Georgios Skretas Prof Ιoannis V Pavlidis Prof Haralambos Stamatis |
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Affiliation: | 1. Biotechnology Laboratory, Department of Biological Applications and Technologies, University of Ioannina, 45110 Ioannina, Greece;2. Institute of Chemical Biology, National Hellenic Research Foundation, 11635 Athens, Greece;3. Department of Medical Physics, School of Health Sciences, University of Ioannina, 45110 Ioannina, Greece;4. Department of Chemistry, University of Crete Voutes, University Campus, 70013 Heraklion, Greece |
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Abstract: | Esterases are among the most studied enzymes, and their applications expand into several branches of industrial biotechnology. Yet, despite the fact that information on their substrate specificity is crucial for selecting or designing the best fitted biocatalyst for the desired application, it cannot be predicted from their amino acid sequence. In this work, we studied the substrate scope of the newly discovered hydrolytic extremozyme, EstDZ3, against a library of esters with variable carbon chain lengths in an effort to understand the crucial amino acids for the substrate selectivity of this enzyme. EstDZ3 appears to be active against a wide range of esters with high selectivity towards medium- to long-carbon chain vinyl esters. In-silico studies of its 3D structure revealed that the selectivity might arise from the mainly hydrophobic nature of the active site's environment. |
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Keywords: | biocatalysis esterases molecular docking molecular dynamics regioselectivity |
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