Bioinformatic evaluation of the substrate specificity exhibited by the highly thermostable esterase EstDZ3
Autor: | Angelos, Papanikolaou, Alexandra V, Chatzikonstantinou, Dimitra, Zarafeta, Nikolaos, Kourkoumelis, Georgios, Skretas, Ioannis V, Pavlidis, Haralambos, Stamatis |
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Rok vydání: | 2022 |
Zdroj: | Chembiochem : a European journal of chemical biology. |
ISSN: | 1439-7633 |
Popis: | Esterases are among the most studied enzymes with applications expanding in several branches of industrial biotechnology. Yet, besides the fact that information on substrate specificity is crucial for selecting or designing the best fitted biocatalyst for the desired application, it cannot be predicted from the amino acid sequence. In the present work, we study the substrate scope of the newly discovered hydrolytic enzyme, EstDZ3, an extremozyme, against a library ofesters with variable carbon chain lengths, in an effort to unveil the 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 revealed that the selectivity may arise from the mainly hydrophobic nature of the active site's environment. |
Databáze: | OpenAIRE |
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