Esterases computational study
Document typeConference report
PublisherBarcelona Supercomputing Center
Rights accessOpen Access
In our project, we are focusing on two different esterases called LAE6 and LAE5. LAE6 is very promiscuous since it presents activity towards a wide range of different substrates, whereas LAE5 presents activity towards few substrates. This promiscuity can be due to the location of the binding cavity: in LAE6 the binding cavity is located buried inside the protein, so the substrates can be retained longer, correlating with a higher reactive probability . LAE5 binding cavity is situated on the surface of the protein, in direct contact with the solvent, which, in our working hypothesis, is the main reason for its much less promiscuity. We are using several computational techniques to extract important descriptors in order to construct a mathematical model to predict the activity of these two enzymes towards different substrates.
CitationCañadas, R.; Santiago, G.; Guallar, V. Esterases computational study. A: BSC Severo Ochoa International Doctoral Symposium (4th: 2017: Barcelona). "Book of abstracts". Barcelona: Barcelona Supercomputing Center, 2017, p. 79-80.