engleski

Theoretical evaluation of enzyme active sites and catalytic peptides involved in ester hydrolysis

A data set was built to analyze enzymes from the EC 3.1. (Hydrolases acting on ester bonds) class looking at both amino acid content and geometry of active site residues. We searched for patterns in existing data by statistically analysing 96 esterases. In this process, 23 enzymes with known catalytic triads were selected for further evaluation. Based on the primary structure of the selected enzymes, the composition profiles were created for: (1) the full sequence, (2) the “long active site” including the residues between the first and the last active amino acid and (3) the “short active site” containing only active residues (catalytic triad and oxyanion hole).

enzymes, active sites, triads

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