Modeling and protein function prediction of truncated form of geobacillus thermocatenulatus lipase (BTL2)

Motivations Lipases, mainly of microbial origin, represent the most widely used class of enzymes in biotechnological applications and organic chemistry. Bacterial lipases are members of the structural superfamily of / hydrolases that catalyze the hydrolysis and synthesis of a variety of acylglycerols at the lipid-water interface. Optimization of features and catalytic activity of lipases as the third industrial enzyme are significant for industrial applications. The structural comparison between / hydrolases and thermoalkalophilic lipases represented that the insertion of Zn2+ binding site ( 3, b1 and b2) has not, until now, been seen within the / hydrolase canonical fold that making a tight intramolecular interaction with the main catalytic domain. In this study, we investigated the role of Zn2+ binding site on lipase activity by using the computational methods.