ProtMiscuity: Promiscuos Proteins Database

VELEZ RUEDA, ANA JULIA; PALOPOLI, NICOLÁS; FORNASARI, SILVINA; PARISI GUSTAVO

Posadas

Congreso; 8CAB2C: 8 Congreso Argentino de Bioinformática y Biología Computacional; 2017

We have developed a database to study the relationship between conformational diversity and protein promiscuity. The database, called ProtMiscuity, was developed through the implementation of web-scraping and text mining techniques. As a result, we obtained 99 entries related to a total of 66 promiscuous proteins with one or more than one characterized promiscuous activities. Catalysed reactions, both promiscuous and canonical, were characterized with all the information available in the literature: substrates,products, Km, Kcat, active site composition and 3D arrangement and reaction conditions. The Protmiscuity is linked with other databases providing additional information such as conformational extension (CoDNaS) and protein function (KEGG, Uniprot , Atlas Catalytic Site, QuickGo) as well as structural details (PDB) for each protein. In addition, substrates and products were related to the information available in PDB Ligand Expo to obtain possible ligands with chemical similarity. A total of 68 different promiscuous reactions were characterized and a final amount of 220 molecules (substrates or products) were related with corresponding reactions. Interestingly, the 32.31% of the proteins in the database have more than one promiscuous associated activity, being the esterase activity the most common promiscuous activity. Protmiscuity could allow users to browse well-curated experimental information that could be used to increase our understanding the underlying mechanisms of protein promiscuity as well to design experiments in industrial, biotechnological and drug design applications.